668:
1432:
1298:
1525:
1510:/IFIH1, all of which are involved in nucleic acid processing. Characterization of mutational distribution in an AGS patient population found 5% of all AGS mutations in RNASEH2A, 36% in 2B, and 12% in 2C. Mutations in 2B have been associated with somewhat milder neurological impairment and with an absence of interferon-induced gene upregulation that can be detected in patients with other AGS-associated genotypes.
7261:
40:
878:
H. Type 1 RNases H have prokaryotic and eukaryotic RNases H1 and retroviral RNase H. Type 2 RNases H have prokaryotic and eukaryotic RNases H2 and bacterial RNase H3. These RNases H exist in a monomeric form, except for eukaryotic RNases H2, which exist in a heterotrimeric form. RNase H1 and H2 have distinct
1665:
may have played a role in establishing the distribution of these enzymes. RNase HI and HIII rarely or never appear in the same prokaryotic genome. When an organism's genome contains more than one RNase H gene, they sometimes have significant differences in activity level. These observations have been
1599:
primer, and removal of the plus-strand purine-rich polypurine tract (PPT) primer. RNase H plays a role in the priming of the plus-strand, but not in the conventional method of synthesizing a new primer sequence. Rather RNase H creates a "primer" from the PPT that is resistant to RNase H cleavage. By
877:
group on either end of the cut site with a two-metal-ion catalysis mechanism, in which two divalent cations, such as Mg2+ and Mn2+, directly participate in the catalytic function. Depending on the differences in their amino acid sequences, these RNases H are classified into type 1 and type 2 RNases
1236:
In prokaryotes, RNase H2 is enzymatically active as a monomeric protein. In eukaryotes, it is an obligate heterotrimer composed of a catalytic subunit A and structural subunits B and C. While the A subunit is closely homologous to the prokaryotic RNase H2, the B and C subunits have no apparent
1435:
The structure of the trimeric human H2 complex, with the catalytic A subunit in blue, the structural B subunit in brown, and the structural C subunit in pink. Although the B and C subunits do not interact with the active site, they are required for activity. The catalytic residues in the
1799:
to facilitate comparative analysis, yielding the modern nomenclature in which the prokaryotic enzymes are designated with Roman numerals and the eukaryotic enzymes with Arabic numerals. The prokaryotic RNase HIII, reported in 1999, was the last RNase H subtype to be identified.
1829:
was sequenced, but the corresponding protein was found not to have enzymatic activity in isolation. Eventually, the yeast B and C subunits were isolated by co-purification and found to be required for enzymatic activity. However, the yeast B and C subunits have very low
1284:
and structural similarity, but have substrate preferences that more closely resemble H1. Unlike HI and HII, which are both widely distributed among prokaryotes, HIII is found in only a few organisms with a scattered taxonomic distribution; it is somewhat more common in
3340:
Ohtani N, Haruki M, Morikawa M, Crouch RJ, Itaya M, Kanaya S (January 1999). "Identification of the genes encoding Mn2+-dependent RNase HII and Mg2+-dependent RNase HIII from
Bacillus subtilis: classification of RNases H into three families".
1639:
that specifically inhibit the polymerase function of RT are in widespread clinical use, but not inhibitors of the RNase H function; it is the only enzymatic function encoded by HIV that is not yet targeted by drugs in clinical use.
1357:
The mechanism of the release of the cleaved product is still unresolved. Experimental evidence from time-resolved crystallography and similar nucleases points to a role of a third ion in the reaction recruited to the active site.
1986:
Crow YJ, Leitch A, Hayward BE, Garner A, Parmar R, Griffith E, et al. (August 2006). "Mutations in genes encoding ribonuclease H2 subunits cause
Aicardi-Goutières syndrome and mimic congenital viral brain infection".
1039:
in a substrate and cannot remove a single ribonucleotide from a strand that is otherwise composed of deoxyribonucleotides. For this reason, it is considered unlikely that RNase H1 enzymes are involved in the processing of
1528:
The crystal structure of the HIV reverse transcriptase heterodimer (yellow and green), with the RNase H domain shown in blue (active site in magenta spheres). The orange nucleic acid strand is RNA, the red strand is
1677:
The evolutionary trajectory of RNase H2 in eukaryotes, especially the mechanism by which eukaryotic homologs became obligate heterotrimers, is unclear; the B and C subunits have no apparent homologs in prokaryotes.
1656:
enzymes and is considered to be evolutionarily ancient. In prokaryotic genomes, multiple RNase H genes are often present, but there is little correlation between occurrence of HI, HII, and HIII genes and overall
4659:
Loo JF, Wang SS, Peng F, He JA, He L, Guo YC, et al. (July 2015). "A non-PCR SPR platform using RNase H to detect MicroRNA 29a-3p from throat swabs of human subjects with influenza A virus H1N1 infection".
2957:"The absence of ribonuclease H1 or H2 alters the sensitivity of Saccharomyces cerevisiae to hydroxyurea, caffeine and ethyl methanesulphonate: implications for roles of RNases H in DNA replication and repair"
839:. Within the H1 group, a relationship has been identified between higher substrate-binding affinity and the presence of structural elements consisting of a helix and flexible loop providing a larger and more
1666:
suggested to reflect an evolutionary pattern that minimizes functional redundancy among RNase H genes. RNase HIII, which is unique to prokaryotes, has a scattered taxonomic distribution and is found in both
1256:
Both prokaryotic and eukaryotic H2 enzymes can cleave single ribonucleotides in a strand. however, they have slightly different cleavage patterns and substrate preferences: prokaryotic enzymes have lower
1280:
Some prokaryotes possess an additional H2-type gene designated RNase HIII in the Roman-numeral nomenclature used for the prokaryotic genes. HIII proteins are more closely related to the H2 group by
1795:
contained two RNase H genes. Originally, the enzyme now known as RNase H2 in eukaryotes was designated H1 and vice versa, but the names of the eukaryotic enzymes were switched to match those in
1576:
are the best-studied members of the family. Retroviral RT is responsible for converting the virus' single-stranded RNA genome into double-stranded DNA. This process requires three steps: first,
2529:
Raschke TM, Marqusee S (April 1997). "The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions".
1342:
is associative in nature and forms an intermediate with protonated phosphate and deprotonated alkoxide leaving group. The leaving group is protonated via the glutamate which has an elevated
4940:
Mölling K, Bolognesi DP, Bauer H, Büsen W, Plassmann HW, Hausen P (December 1971). "Association of viral reverse transcriptase with an enzyme degrading the RNA moiety of RNA-DNA hybrids".
4222:
Mizuno M, Yasukawa K, Inouye K (February 2010). "Insight into the mechanism of the stabilization of moloney murine leukaemia virus reverse transcriptase by eliminating RNase H activity".
1265:
deoxyribonucleotide, while eukaryotic enzymes are more processive and hydrolyze both types of substrate with similar efficiency. The substrate specificity of RNase H2 gives it a role in
5265:
Frank P, Braunshofer-Reiter C, Wintersberger U (January 1998). "Yeast RNase H(35) is the counterpart of the mammalian RNase HI, and is evolutionarily related to prokaryotic RNase HII".
3673:
Reus K, Mayer J, Sauter M, Scherer D, MĂĽller-Lantzsch N, Meese E (March 2001). "Genomic organization of the human endogenous retrovirus HERV-K(HML-2.HOM) (ERVK6) on chromosome 7".
1588:
activity synthesizes plus-strand DNA, generating double-stranded DNA as the final product. The second step of this process is carried out by an RNase H domain located at the
3853:"The structural and biochemical characterization of human RNase H2 complex reveals the molecular basis for substrate recognition and Aicardi-Goutières syndrome defects"
2800:"The structural and biochemical characterization of human RNase H2 complex reveals the molecular basis for substrate recognition and Aicardi-Goutières syndrome defects"
382:
1204:
999:
211:
485:
encodes both H1 and H2. Human ribonuclease H2 is a heterotrimeric complex composed of three subunits, mutations in any of which are among the genetic causes of a
401:
230:
1338:
Based on experimental evidence and computer simulations the enzyme activates a water molecule bound to one of the metal ions with the conserved histidine. The
1834:
to their homologs in other organisms, and the corresponding human proteins were conclusively identified only after mutations in all three were found to cause
1461:
2211:
Tadokoro T, Kanaya S (March 2009). "Ribonuclease H: molecular diversities, substrate binding domains, and catalytic mechanism of the prokaryotic enzymes".
2091:
Davies JF, Hostomska Z, Hostomsky Z, Jordan SR, Matthews DA (April 1991). "Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase".
1490:
symptoms at an early age. The symptoms of AGS closely resemble those of congenital viral infection and are associated with inappropriate upregulation of
4404:
Klarmann GJ, Hawkins ME, Le Grice SF (2002). "Uncovering the complexities of retroviral ribonuclease H reveals its potential as a therapeutic target".
5388:
4711:
Goodrich TT, Lee HJ, Corn RM (April 2004). "Direct detection of genomic DNA by enzymatically amplified SPR imaging measurements of RNA microarrays".
886:, whereas both are believed to be essential in higher eukaryotes. The combined activity of both H1 and H2 enzymes is associated with maintenance of
4181:
Moelling K, Broecker F, Kerrigan JE (2014-01-01). "RNase H: Specificity, Mechanisms of Action, and
Antiviral Target". In Vicenzi E, Poli G (eds.).
1710:. It can also be used to cleave specific RNA sequences in the presence of short complementary segments of DNA. Highly sensitive techniques such as
6335:
825:
RNases H1 have been extensively studied to explore the relationships between structure and enzymatic activity. They are also used, especially the
4807:
Stein H, Hausen P (October 1969). "Enzyme from calf thymus degrading the RNA moiety of DNA-RNA Hybrids: effect on DNA-dependent RNA polymerase".
6582:
5952:
5915:
1595:
RNase H performs three types of cleaving actions: non-specific degradation of the plus-strand RNA genome, specific removal of the minus-strand
2443:
Cecconi C, Shank EA, Bustamante C, Marqusee S (September 2005). "Direct observation of the three-state folding of a single protein molecule".
814:. Prokaryotic HIII enzymes are members of the broader H2 group and share most structural features with H2, with the addition of an N-terminal
5182:
4607:
4334:
4198:
3119:
6496:
810:. While all members of the H1 group and the prokaryotic members of the H2 group function as monomers, eukaryotic H2 enzymes are obligate
6597:
6591:
6392:
6142:
3991:"Characterization of human disease phenotypes associated with mutations in TREX1, RNASEH2A, RNASEH2B, RNASEH2C, SAMHD1, ADAR, and IFIH1"
802:
organization of the enzymes varies; some prokaryotic and most eukaryotic members of the H1 group have an additional small domain at the
6440:
6035:
4466:
Cao L, Song W, De Clercq E, Zhan P, Liu X (June 2014). "Recent progress in the research of small molecule HIV-1 RNase H inhibitors".
1835:
1479:
490:
6980:
6551:
6340:
6044:
5610:
619:
RNases H can be broadly divided into two subtypes, H1 and H2, which for historical reasons are given Arabic numeral designations in
4758:"RNase H-dependent PCR (rhPCR): improved specificity and single nucleotide polymorphism detection using blocked cleavable primers"
3142:"Contributions of the two accessory subunits, RNASEH2B and RNASEH2C, to the activity and properties of the human RNase H2 complex"
1584:
DNA from the plus-strand RNA template, generating an RNA:DNA hybrid intermediate; second, the RNA strand is destroyed; and third,
394:
6097:
1636:
1076:
223:
6658:
6546:
847:
and human RNase H1 homologs and absent in the HIV RNase H domain, but examples of retroviral domains with C-helices do exist.
361:
6467:
6377:
6330:
5957:
337:
174:
150:
7136:
1224:
1019:
806:
known as the "hybrid binding domain", which facilitates binding to RNA:DNA hybrid duplexes and sometimes confers increased
6889:
6830:
5767:
5617:
5381:
7251:
5165:
Crouch RJ, Arudchandran A, Cerritelli SM (2001-01-01). "RNase H1 of
Saccharomyces cerevisiae: methods and nomenclature".
4431:
Tramontano E, Di Santo R (2010). "HIV-1 RT-associated RNase H function inhibitors: Recent advances in drug development".
4317:
Nowotny M, Figiel M (2013-01-01). "The RNase H Domain: Structure, Function and
Mechanism". In LeGrice S, Gotte M (eds.).
6934:
6501:
6491:
1585:
1577:
1554:
882:
preferences and distinct but overlapping functions in the cell. In prokaryotes and lower eukaryotes, neither enzyme is
6894:
6786:
6411:
5758:
5426:
5401:
1803:
Characterizing eukaryotic RNase H2 was historically a challenge, in part due to its low abundance. Careful efforts at
1453:
1404:
1242:
713:
593:
3231:"RNase H and multiple RNA biogenesis factors cooperate to prevent RNA:DNA hybrids from generating genome instability"
1448:
at position 177 of subunit B - is shown as a green sphere. Many of these mutations do not disrupt catalytic activity
4501:
Ma BG, Chen L, Ji HF, Chen ZH, Yang FR, Wang L, et al. (February 2008). "Characters of very ancient proteins".
1864:
Goedken ER, Marqusee S (December 2001). "Native-state energetics of a thermostabilized variant of ribonuclease HI".
6480:
6476:
6472:
6388:
6221:
5887:
5863:
5732:
5564:
5511:
5493:
5405:
1702:
RNase HI and HII are commercially available. RNase HI is often used to destroy the RNA template after first-strand
1440:
are shown in magenta. Positions shown in yellow are those with known AGS mutations. The most common AGS mutation -
1323:
The charged residues bind two metal ions that are required for catalysis; under physiological conditions these are
1266:
679:
proteins, the structural core common between the H1 and H2 subtypes is shown in red. Structures are rendered from:
7121:
5108:"Isolation and characterization of a second RNase H (RNase HII) of Escherichia coli K-12 encoded by the rnhB gene"
1545:, which encode their genomes in single-stranded RNA and replicate through a double-stranded DNA intermediate; and
7237:
7224:
7211:
7198:
7185:
7172:
7159:
6742:
6688:
6648:
6607:
6511:
6350:
6318:
6204:
6168:
5941:
3445:"Evidence for a dual functional role of a conserved histidine in RNA·DNA heteroduplex cleavage by human RNase H1"
2494:
Hollien J, Marqusee S (March 1999). "A thermodynamic comparison of mesophilic and thermophilic ribonucleases H".
1711:
1658:
1581:
1519:
502:
355:
7131:
2905:"Viable RNaseH1 knockout mice show RNaseH1 is essential for R loop processing, mitochondrial and liver function"
2348:
Schmitt TJ, Clark JE, Knotts TA (December 2009). "Thermal and mechanical multistate folding of ribonuclease H".
1791:. It later became clear that calf thymus extract contained more than one protein with RNase H activity and that
1686:
Because RNase H specifically degrades only the RNA in double-stranded RNA:DNA hybrids, it is commonly used as a
1423:
are also common in the genome and often include their own RNase H domains, with a complex evolutionary history.
168:
7085:
7028:
6396:
6245:
6159:
6102:
5374:
5360:
1662:
815:
260:
61:
1316:
of nearly all RNases H contains four negatively charged amino acid residues, known as the DEDD motif; often a
1212:
1007:
342:
2257:
Majorek KA, Dunin-Horkawicz S, Steczkiewicz K, Muszewska A, Nowotny M, Ginalski K, Bujnicki JM (April 2014).
155:
7033:
6265:
6135:
5504:
5435:
5208:"Cloning of the cDNA encoding the large subunit of human RNase HI, a homologue of the prokaryotic RNase HII"
2259:"The RNase H-like superfamily: new members, comparative structural analysis and evolutionary classification"
3989:
Crow YJ, Chase DS, Lowenstein
Schmidt J, Szynkiewicz M, Forte GM, Gornall HL, et al. (February 2015).
7281:
6821:
6460:
6001:
5932:
4720:
3544:
DĂĽrr S, Bohusewicz O, Berta D, Suardiaz R, Peter C, Jambrina PG, Peter C, Shao Y, Rosta E (16 June 2021).
2037:"Crystal structure of RNase H3-substrate complex reveals parallel evolution of RNA/DNA hybrid recognition"
1739:
580:
group. RNases H have been proposed as members of an evolutionarily related superfamily encompassing other
406:
1277:, H2 is the dominant source of RNase H activity there and is important for maintaining genome stability.
330:
235:
7054:
6973:
6756:
6653:
6445:
6406:
6270:
6192:
5927:
5696:
5366:
1788:
1723:
1707:
1573:
1562:
1538:
1465:
1408:
1107:. The defects in mitochondrial DNA replication induced by loss of RNase H1 are likely due to defects in
879:
819:
667:
548:
506:
478:
452:
143:
7126:
1208:
1003:
3094:
Hollis T, Shaban NM (2011-01-01). "Structure and
Function of RNase H Enzymes". In Nicholson AW (ed.).
6939:
6774:
6769:
6702:
6362:
6187:
5974:
5947:
5898:
5219:
5119:
4816:
4669:
4267:"Murine leukemia virus reverse transcriptase: structural comparison with HIV-1 reverse transcriptase"
3394:
3291:
2452:
2357:
2100:
1804:
1695:
1601:
1416:
585:
525:
78:
4725:
1742:
protein commonly used as a reagent is not effective at inhibiting the activity of either HI or HII.
843:
substrate-binding surface. The C-helix has a scattered taxonomic distribution; it is present in the
358:
7090:
6794:
6764:
6568:
6563:
6487:
6423:
6209:
5704:
3546:"The Role of Conserved Residues in the DEDDh Motif: the Proton-Transfer Mechanism of HIV-1 RNase H"
1628:
791:
residues, often referred to as the DEDD motif. These residues interact with catalytically required
697:
430:
282:
171:
73:
3042:"RNASEH1 Mutations Impair mtDNA Replication and Cause Adult-Onset Mitochondrial Encephalomyopathy"
2955:
Arudchandran A, Cerritelli S, Narimatsu S, Itaya M, Shin DY, Shimada Y, Crouch RJ (October 2000).
95:
7286:
7023:
6927:
6779:
6260:
6250:
6128:
4840:
4693:
4633:
4621:
4247:
3971:
3833:
3565:
2623:"Ribonuclease H: properties, substrate specificity and roles in retroviral reverse transcription"
2554:
2476:
2236:
2012:
1687:
1301:
671:
Comparison of the structures of representative ribonuclease H proteins from each subtype. In the
459:
1607:
Because RNase H activity is required for viral proliferation, this domain has been considered a
1600:
removing all bases but the PPT, the PPT is used as a marker for the end of the U3 region of its
675:
protein (beige, top left), the four conserved active site residues are shown as spheres. In the
3103:
6728:
6673:
6641:
6516:
6235:
5910:
5727:
5331:
5282:
5247:
5188:
5178:
5147:
5088:
5047:
5006:
4957:
4922:
4881:
4832:
4789:
4738:
4685:
4613:
4603:
4567:
4518:
4483:
4448:
4413:
4386:
4330:
4296:
4239:
4204:
4194:
4163:
4118:
4069:
4020:
3963:
3946:
Crow YJ, Manel N (July 2015). "Aicardi-Goutières syndrome and the type I interferonopathies".
3925:
3884:
3825:
3790:
3741:
3690:
3655:
3606:
3545:
3523:
3474:
3422:
3358:
3317:
3260:
3211:
3171:
3115:
3071:
3019:
2978:
2934:
2882:
2831:
2780:
2731:
2714:
Ohtani N, Haruki M, Morikawa M, Kanaya S (January 1999). "Molecular diversities of RNases H".
2696:
2652:
2603:
2546:
2511:
2468:
2425:
2373:
2330:
2288:
2228:
2168:
2116:
2066:
2004:
1963:
1881:
1854:
1831:
1734:
1727:
1703:
1691:
1558:
1491:
1281:
1238:
1199:
1104:
994:
840:
764:
751:
735:
719:
703:
687:
349:
162:
4089:"Crystal structure of HIV-1 reverse transcriptase in complex with a polypurine tract RNA:DNA"
3140:
Chon H, Vassilev A, DePamphilis ML, Zhao Y, Zhang J, Burgers PM, et al. (January 2009).
1718:
or to introduce single-stranded nicks at positions containing a ribonucleotide. A variant of
1549:, which replicate their double-stranded DNA genomes through an RNA "pregenome" intermediate.
7069:
7064:
7038:
6966:
6804:
6384:
6289:
6284:
6240:
5867:
5716:
5711:
5603:
5321:
5313:
5274:
5237:
5227:
5170:
5137:
5127:
5078:
5037:
4996:
4988:
4949:
4912:
4871:
4824:
4779:
4769:
4730:
4677:
4595:
4557:
4549:
4510:
4475:
4440:
4376:
4366:
4322:
4286:
4278:
4231:
4186:
4153:
4145:
4108:
4100:
4059:
4051:
4010:
4002:
3955:
3915:
3874:
3864:
3817:
3780:
3772:
3731:
3721:
3682:
3645:
3637:
3596:
3557:
3513:
3505:
3464:
3456:
3412:
3402:
3350:
3307:
3299:
3250:
3242:
3203:
3161:
3153:
3107:
3095:
3061:
3053:
3040:
Reyes A, Melchionda L, Nasca A, Carrara F, Lamantea E, Zanolini A, et al. (July 2015).
3009:
2968:
2924:
2916:
2872:
2862:
2821:
2811:
2770:
2762:
2723:
2686:
2642:
2634:
2593:
2585:
2538:
2503:
2460:
2415:
2407:
2365:
2322:
2278:
2270:
2220:
2158:
2150:
2108:
2056:
2048:
1996:
1953:
1945:
1873:
1715:
1620:
1475:
1431:
1339:
1045:
832:
629:
318:
46:
4087:
Sarafianos SG, Das K, Tantillo C, Clark AD, Ding J, Whitcomb JM, et al. (March 2001).
1714:
can be used for detection. RNase HII can be used to degrade the RNA primer component of an
1524:
1191:
986:
131:
7116:
7100:
7013:
6906:
6720:
6636:
6631:
6626:
6539:
6534:
6294:
6172:
6080:
5872:
5746:
5464:
5414:
5397:
4645:
3383:"Evolution of ribonuclease H genes in prokaryotes to avoid inheritance of redundant genes"
2998:"Failure to produce mitochondrial DNA results in embryonic lethality in Rnaseh1 null mice"
2396:"Specific recognition of RNA/DNA hybrid and enhancement of human RNase H1 activity by HBD"
1649:
1420:
1250:
1080:
1049:
836:
521:
498:
294:
265:
107:
5223:
5123:
4820:
4673:
3398:
3295:
2456:
2361:
2104:
1052:. RNase H1 is not essential in unicellular organisms where it has been investigated; in
66:
7265:
7154:
7095:
6879:
6874:
6869:
6255:
6230:
6226:
6199:
6182:
5720:
5700:
5042:
5025:
4876:
4859:
4784:
4757:
4562:
4537:
4381:
4354:
4291:
4266:
4158:
4137:
4064:
4039:
4038:
Rice G, Patrick T, Parmar R, Taylor CF, Aeby A, Aicardi J, et al. (October 2007).
4015:
3990:
3879:
3852:
3785:
3760:
3736:
3709:
3650:
3625:
3518:
3493:
3469:
3444:
3417:
3382:
3312:
3279:
3255:
3230:
3166:
3141:
3066:
3041:
2929:
2904:
2877:
2850:
2826:
2799:
2775:
2750:
2647:
2622:
2598:
2573:
2420:
2395:
2283:
2258:
2154:
2061:
2036:
1958:
1933:
1822:
1612:
1546:
1092:
1032:
883:
856:
811:
799:
780:
563:
377:
206:
5326:
5301:
5278:
5174:
5083:
5066:
5001:
4976:
4917:
4900:
4756:
Dobosy JR, Rose SD, Beltz KR, Rupp SM, Powers KM, Behlke MA, Walder JA (August 2011).
4479:
4113:
4088:
3014:
2997:
2727:
2394:
Nowotny M, Cerritelli SM, Ghirlando R, Gaidamakov SA, Crouch RJ, Yang W (April 2008).
2326:
2163:
2138:
1261:
and hydrolyze successive ribonucleotides more efficiently than ribonucleotides with a
7275:
7059:
7018:
6620:
6529:
6279:
5922:
5849:
5459:
5242:
5207:
5142:
5107:
4625:
3601:
3584:
3569:
3096:
2973:
2903:
Lima WF, Murray HM, Damle SS, Hart CE, Hung G, De Hoyos CL, et al. (June 2016).
2675:"Making and breaking nucleic acids: two-Mg2+-ion catalysis and substrate specificity"
2638:
2224:
1949:
1813:
1759:
1719:
1100:
1096:
1064:
1059:
186:
181:
4992:
4977:"Ribonuclease H: a ubiquitous activity in virions of ribonucleic acid tumor viruses"
4844:
4697:
4251:
3975:
2558:
2480:
2240:
2139:"Identification and characterization of HIV-specific RNase H by monoclonal antibody"
1471:
Mutations in any of the three RNase H2 subunits are well-established as causes of a
1140:
923:
7008:
6747:
6678:
6401:
6322:
6061:
5356:
4282:
3837:
2589:
2016:
1755:
1751:
1472:
1367:
1274:
1258:
1187:
1088:
1084:
982:
807:
635:
559:
541:
486:
482:
434:
4901:"Ribonuclease H (hybrid) in Escherichia coli. Identification and characterization"
1403:
origin appears frequently in the genome, reflecting integration of the genomes of
1297:
1153:
936:
772:
5206:
Frank P, Braunshofer-Reiter C, Wintersberger U, Grimm R, BĂĽsen W (October 1998).
4828:
4599:
3761:"Convergent evolution of ribonuclease h in LTR retrotransposons and retroviruses"
3246:
3111:
2691:
2674:
2574:"RNase H activity: structure, specificity, and function in reverse transcription"
1165:
948:
477:
The family is divided into evolutionarily related groups with slightly different
7232:
7167:
7003:
6922:
6693:
6587:
6450:
6416:
6354:
6120:
6006:
4536:
Brindefalk B, Dessailly BH, Yeats C, Orengo C, Werner F, Poole AM (March 2013).
4326:
4190:
4149:
3851:
Figiel M, Chon H, Cerritelli SM, Cybulska M, Crouch RJ, Nowotny M (March 2011).
3278:
Kim N, Huang SN, Williams JS, Li YC, Clark AB, Cho JE, et al. (June 2011).
2996:
Cerritelli SM, Frolova EG, Feng C, Grinberg A, Love PE, Crouch RJ (March 2003).
2798:
Figiel M, Chon H, Cerritelli SM, Cybulska M, Crouch RJ, Nowotny M (March 2011).
1608:
1487:
1437:
1313:
776:
609:
605:
589:
528:. Both H1 and H2 are involved in genome maintenance tasks such as processing of
7260:
5212:
Proceedings of the
National Academy of Sciences of the United States of America
5112:
Proceedings of the
National Academy of Sciences of the United States of America
4514:
4444:
3057:
2751:"PCNA directs type 2 RNase H activity on DNA replication and repair substrates"
190:
6899:
6092:
6066:
5854:
5839:
5351:
4185:. Methods in Molecular Biology. Vol. 1087. Humana Press. pp. 71–84.
4104:
3726:
3641:
3194:
Reijns MA, Jackson AP (August 2014). "Ribonuclease H2 in health and disease".
1589:
1542:
1407:. Such integration events result in the presence of genes encoding retroviral
1400:
1041:
803:
768:
745:
729:
624:
510:
494:
456:
5232:
3561:
1083:
with and without the MTS present. As a result, RNase H1 is localized to both
7206:
7180:
6812:
6611:
6524:
6151:
6030:
5844:
5834:
5132:
4774:
3869:
3776:
3407:
3303:
3102:. Nucleic Acids and Molecular Biology. Springer Berlin Heidelberg. pp.
2816:
2749:
Bubeck D, Reijns MA, Graham SC, Astell KR, Jones EY, Jackson AP (May 2011).
2464:
2112:
1784:
1780:
1632:
1624:
1483:
1445:
1328:
1324:
1317:
1036:
874:
792:
788:
784:
620:
601:
577:
471:
462:. Members of the RNase H family can be found in nearly all organisms, from
441:
5335:
5192:
4953:
4793:
4742:
4689:
4617:
4571:
4522:
4487:
4452:
4417:
4390:
4300:
4243:
4208:
4167:
4122:
4073:
4024:
3967:
3929:
3888:
3829:
3808:
Malik HS (2005). "Ribonuclease H evolution in retrotransposable elements".
3794:
3745:
3694:
3686:
3659:
3610:
3527:
3478:
3426:
3321:
3264:
3215:
3175:
3075:
3023:
2982:
2938:
2886:
2835:
2784:
2735:
2700:
2656:
2607:
2515:
2472:
2429:
2377:
2292:
2232:
2070:
2008:
1967:
1885:
1877:
5286:
5251:
5151:
5092:
5010:
4961:
4926:
4885:
4836:
3362:
2550:
2411:
2334:
2274:
2172:
2120:
6857:
6852:
6847:
6668:
6303:
6155:
6107:
6088:
5660:
5651:
5449:
5317:
4553:
4006:
3920:
3903:
3585:"A stepwise model for double-stranded RNA processing by ribonuclease III"
3280:"Mutagenic processing of ribonucleotides in DNA by yeast topoisomerase I"
3157:
2920:
2766:
2052:
1730:
1667:
1653:
1616:
1550:
1392:
1386:
1380:
1160:
943:
867:
652:
581:
570:
463:
306:
5051:
3207:
2867:
2542:
1460:
In small studies, mutations in human RNase H1 have been associated with
119:
39:
6864:
6842:
6837:
6455:
5671:
5646:
5641:
5473:
4860:"Ribonuclease H. An enzyme degrading the RNA moiety of DNA-RNA hybrids"
4681:
3460:
1775:
1671:
1441:
1374:
1347:
1332:
1286:
1054:
955:
827:
681:
656:
467:
325:
138:
17:
5300:
Jeong HS, Backlund PS, Chen HC, Karavanov AA, Crouch RJ (2004-01-01).
4734:
4594:. Vol. Chapter 3. John Wiley & Sons, Inc. pp. Unit3.13.
4235:
3821:
3509:
3354:
2507:
2369:
1858:
1354:
enzyme which both also use a histidine and a two-metal ion mechanism.
798:
RNases H2 are larger than H1 and usually have additional helices. The
755:
739:
723:
707:
691:
651:
gene encodes HII. A third related class, called HIII, occurs in a few
7219:
6989:
6884:
6817:
6710:
6308:
6216:
5302:"RNase H2 of Saccharomyces cerevisiae is a complex of three proteins"
5067:"DNA sequence of the gene coding for Escherichia coli ribonuclease H"
4371:
4355:"HIV-1 Ribonuclease H: Structure, Catalytic Mechanism and Inhibitors"
1826:
1762:
1726:
or rhPCR, has been described using a thermostable RNase HII from the
1499:
1270:
1219:
1108:
1072:
1014:
960:
891:
887:
544:
529:
437:
389:
301:
289:
277:
218:
114:
102:
90:
3959:
2310:
1269:, removing misincorporated ribonucleotides from DNA, in addition to
4055:
3583:
Gan J, Shaw G, Tropea JE, Waugh DS, Court DL, Ji X (January 2008).
2956:
2000:
1289:
and is rarely or never found in the same prokaryotic genome as HI.
7193:
6826:
6577:
6573:
6021:
6016:
6011:
5994:
5989:
5984:
5979:
5967:
5962:
5680:
5675:
5632:
5627:
5622:
1569:
1534:
1523:
1495:
1430:
1412:
1305:
1296:
1262:
890:
stability due to the enzymes' degradation of the RNA component of
871:
864:
666:
574:
567:
1273:
processing. Although both H1 and H2 are present in the mammalian
6558:
6435:
6428:
6372:
6367:
5903:
5827:
5822:
5817:
5812:
5807:
5802:
5797:
5792:
5787:
5782:
5777:
5772:
5664:
5594:
5589:
5584:
5579:
5574:
5569:
5557:
5550:
5541:
5536:
5531:
5526:
5521:
5516:
5478:
5454:
5442:
4040:"Clinical and molecular phenotype of Aicardi-Goutieres syndrome"
1596:
1507:
1503:
1351:
1246:
1181:
1147:
1135:
976:
930:
918:
613:
597:
313:
126:
6962:
6124:
5370:
3494:"Calcium inhibition of ribonuclease H1 two-metal ion catalysis"
2851:"RNase H enables efficient repair of R-loop induced DNA damage"
1821:
protein (that is, the H2A subunit) was easily identifiable by
1346:
and is likely to be protonated. The mechanism is similar to
1343:
860:
556:
552:
514:
493:. A third type, closely related to H2, is found only in a few
449:
445:
3759:
Ustyantsev K, Novikova O, Blinov A, Smyshlyaev G (May 2015).
1773:
specificity. RNase H activity was subsequently discovered in
3229:
Wahba L, Amon JD, Koshland D, Vuica-Ross M (December 2011).
481:
preferences, broadly designated ribonuclease H1 and H2. The
5352:
GeneReviews/NCBI/NIH/UW entry on
Aicardi-Goutières Syndrome
2137:
Hansen J, Schulze T, Mellert W, Moelling K (January 1988).
1811:
RNase H2, the eukaryotic enzyme had multiple subunits. The
1750:
Ribonucleases H were first discovered in the laboratory of
6958:
5169:. Methods in Enzymology. Vol. 341. pp. 395–413.
822:
proteins have structures closely resembling the H1 group.
3710:"Convergence of retrotransposons in oomycetes and plants"
1674:; it is believed to have diverged from HII fairly early.
1237:
homologs in prokaryotes and are poorly conserved at the
3708:
Ustyantsev K, Blinov A, Smyshlyaev G (14 March 2017).
1494:. AGS can also be caused by mutations in other genes:
818:. Retroviral RNase H domains occurring in multidomain
7249:
4975:
Grandgenett DP, Gerard GF, Green M (December 1972).
4538:"Evolutionary history of the TBP-domain superfamily"
2950:
2948:
1241:
level even among eukaryotes. The B subunit mediates
659:; it is closely related to prokaryotic HII enzymes.
7145:
7109:
7078:
7047:
6996:
6915:
6803:
6755:
6741:
6719:
6701:
6687:
6667:
6606:
6510:
6349:
6317:
6167:
6079:
6053:
5883:
5754:
5745:
5689:
5489:
5422:
5413:
5026:"Distinct ribonuclease H activities in calf thymus"
4503:
Biochemical and Biophysical Research Communications
1452:, but do destabilize the complex or interfere with
1218:
1198:
1180:
1175:
1159:
1146:
1134:
1126:
1121:
1013:
993:
975:
970:
954:
942:
929:
917:
909:
904:
400:
388:
376:
371:
348:
336:
324:
312:
300:
288:
276:
271:
259:
254:
249:
229:
217:
205:
200:
180:
161:
149:
137:
125:
113:
101:
89:
84:
72:
60:
55:
32:
4319:Human Immunodeficiency Virus Reverse Transcriptase
4138:"Molecular biology of hepatitis B virus infection"
1927:
1925:
1923:
1921:
1919:
1917:
1915:
1561:, respectively. Both encode large multifunctional
1411:, which includes an RNase H domain. An example is
1383:, the catalytic subunit of the trimeric H2 complex
1304:for RNase H catalysis using two metal ions in the
6446:Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase
4348:
4346:
1913:
1911:
1909:
1907:
1905:
1903:
1901:
1899:
1897:
1895:
1648:RNases H are widely distributed and occur in all
1395:, a structural subunit of the trimeric H2 complex
1389:, a structural subunit of the trimeric H2 complex
1335:or high concentration of Mg2+ inhibits activity.
1320:e.g. in HIV-1, human or E. coli is also present.
1062:confer a temperature-sensitive phenotype, and in
2206:
2204:
2202:
1652:. The family belongs to a larger superfamily of
1331:also usually supports enzymatic activity, while
4585:
4583:
4581:
4312:
4310:
3376:
3374:
3372:
2389:
2387:
2200:
2198:
2196:
2194:
2192:
2190:
2188:
2186:
2184:
2182:
863:in a double-stranded RNA:DNA hybrid, leaving a
3335:
3333:
3331:
3189:
3187:
3185:
3089:
3087:
3085:
2309:Rice P, Craigie R, Davies DR (February 1996).
2252:
2250:
1031:Ribonuclease H1 enzymes require at least four
562:. By definition, RNases H cleave RNA backbone
520:In eukaryotes, ribonuclease H1 is involved in
6974:
6136:
5382:
3539:
3537:
3035:
3033:
2132:
2130:
2086:
2084:
2082:
2080:
2030:
2028:
2026:
1619:and other conditions caused by retroviruses.
1419:(LTR) and non-long terminal repeat (non-LTR)
767:of RNase H commonly consists of a 5-stranded
8:
3995:American Journal of Medical Genetics. Part A
3941:
3939:
3438:
3436:
3135:
3133:
3131:
2898:
2896:
2668:
2666:
1462:chronic progressive external ophthalmoplegia
584:and nucleic acid processing enzymes such as
4899:Miller HI, Riggs AD, Gill GN (April 1973).
4224:Bioscience, Biotechnology, and Biochemistry
3626:"Cation trafficking propels RNA hydrolysis"
3492:Rosta E, Yang W, Hummer G (February 2014).
2304:
2302:
1981:
1979:
1977:
1934:"Ribonuclease H: the enzymes in eukaryotes"
1765:in 1969 and gave it the name "ribonuclease
1627:have been identified, many of which have a
1623:of retroviral RNase H of several different
1068:, they produce defects in stress response.
6981:
6967:
6959:
6752:
6698:
6684:
6143:
6129:
6121:
5751:
5419:
5389:
5375:
5367:
3381:Kochiwa H, Tomita M, Kanai A (July 2007).
1565:(RT) proteins containing RNase H domains.
1377:, an example of the H1 (monomeric) subtype
1172:
967:
368:
197:
38:
5359:at the U.S. National Library of Medicine
5325:
5241:
5231:
5141:
5131:
5082:
5041:
5000:
4916:
4875:
4783:
4773:
4724:
4561:
4380:
4370:
4290:
4157:
4112:
4063:
4014:
3919:
3878:
3868:
3784:
3735:
3725:
3649:
3630:Nature Structural & Molecular Biology
3600:
3517:
3468:
3416:
3406:
3311:
3254:
3165:
3065:
3013:
2972:
2928:
2876:
2866:
2825:
2815:
2774:
2690:
2646:
2597:
2419:
2311:"Retroviral integrases and their cousins"
2282:
2162:
2060:
1957:
1807:of the enzyme suggested that, unlike the
4713:Journal of the American Chemical Society
3498:Journal of the American Chemical Society
2716:Journal of Bioscience and Bioengineering
2673:Yang W, Lee JY, Nowotny M (April 2006).
517:and are required for viral replication.
7256:
6336:Ubiquitin carboxy-terminal hydrolase L1
3443:Alla NR, Nicholson AW (December 2012).
1932:Cerritelli SM, Crouch RJ (March 2009).
1846:
4641:
4631:
3902:Orcesi S, La Piana R, Fazzi E (2009).
2621:Champoux JJ, Schultz SJ (March 2009).
1754:when researchers found RNA:DNA hybrid
1370:contains four genes encoding RNase H:
1118:
901:
246:
29:
6916:either deoxy- or ribo-
4321:. Springer New York. pp. 53–75.
2849:Amon JD, Koshland D (December 2016).
2572:Schultz SJ, Champoux JJ (June 2008).
2315:Current Opinion in Structural Biology
7:
6497:Protein serine/threonine phosphatase
5065:Kanaya S, Crouch RJ (January 1983).
4353:Beilhartz GL, Götte M (April 2010).
6598:Cyclic nucleotide phosphodiesterase
6592:Clostridium perfringens alpha toxin
6393:Tartrate-resistant acid phosphatase
5071:The Journal of Biological Chemistry
4905:The Journal of Biological Chemistry
3857:The Journal of Biological Chemistry
2804:The Journal of Biological Chemistry
2035:Figiel M, Nowotny M (August 2014).
6441:Pyruvate dehydrogenase phosphatase
5043:10.1111/j.1432-1033.1975.tb03985.x
4877:10.1111/j.1432-1033.1970.tb00287.x
4044:American Journal of Human Genetics
3046:American Journal of Human Genetics
2155:10.1002/j.1460-2075.1988.tb02805.x
1095:models, RNase H1-null mutants are
855:Ribonuclease H enzymes cleave the
623:and Roman numeral designations in
551:specificity for the RNA strand of
25:
6341:4-hydroxybenzoyl-CoA thioesterase
6045:Control of chromosome duplication
5611:Autonomously replicating sequence
4480:10.2174/0929867321666140120121158
3624:Samara NL, Yang W (August 2019).
1399:In addition, genetic material of
497:, whereas H1 and H2 occur in all
7259:
5030:European Journal of Biochemistry
5024:BĂĽsen W, Hausen P (March 1975).
4864:European Journal of Biochemistry
4590:Nichols NM, Yue D (2001-01-01).
3602:10.1111/j.1365-2958.2007.06032.x
3196:Biochemical Society Transactions
2974:10.1046/j.1365-2443.2000.00373.x
2639:10.1111/j.1742-4658.2009.06909.x
2225:10.1111/j.1742-4658.2009.06907.x
1950:10.1111/j.1742-4658.2009.06908.x
1637:Reverse-transcriptase inhibitors
1456:with other proteins in the cell.
1077:mitochondrial targeting sequence
771:surrounded by a distribution of
643:and many other prokaryotes, the
6659:N-acetylglucosamine-6-sulfatase
6547:Sphingomyelin phosphodiesterase
4993:10.1128/jvi.10.6.1136-1142.1972
4858:Hausen P, Stein H (June 1970).
4136:Seeger C, Mason WS (May 2015).
3810:Cytogenetic and Genome Research
3765:Molecular Biology and Evolution
2350:The Journal of Chemical Physics
1615:drugs used in the treatment of
536:Classification and nomenclature
509:proteins, which are encoded by
6468:Inositol-phosphate phosphatase
6331:Palmitoyl protein thioesterase
4283:10.1016/j.virusres.2008.01.001
4265:Coté ML, Roth MJ (June 2008).
2590:10.1016/j.virusres.2007.12.007
1787:during early studies of viral
1541:as part of their life cycles:
1267:ribonucleotide excision repair
1103:due to defects in replicating
1071:In many eukaryotes, including
540:Ribonuclease H is a family of
501:. Additionally, RNase H1-like
44:Crystallographic structure of
1:
6831:RNA-induced silencing complex
5768:DNA polymerase III holoenzyme
5618:Single-strand binding protein
5279:10.1016/s0014-5793(97)01528-7
5175:10.1016/s0076-6879(01)41166-9
5084:10.1016/S0021-9258(18)33189-2
4918:10.1016/S0021-9258(19)44152-5
3015:10.1016/s1097-2765(03)00088-1
2728:10.1016/s1389-1723(99)80168-6
2327:10.1016/s0959-440x(96)80098-4
1405:human endogenous retroviruses
1176:Available protein structures:
971:Available protein structures:
633:RNase HI is a homolog of the
505:domains occur in multidomain
6935:Serratia marcescens nuclease
6502:Dual-specificity phosphatase
6492:Protein tyrosine phosphatase
4829:10.1126/science.166.3903.393
4600:10.1002/0471142727.mb0313s84
3904:"Aicardi-Goutieres syndrome"
3247:10.1016/j.molcel.2011.10.017
3112:10.1007/978-3-642-21078-5_12
2692:10.1016/j.molcel.2006.03.013
1866:Journal of Molecular Biology
1635:of the active-site cations.
1586:DNA-dependent DNA polymerase
1578:RNA-dependent DNA polymerase
1568:Retroviral RT proteins from
1555:human immunodeficiency virus
1454:protein-protein interactions
1350:and the RuvC subunit in the
1243:protein-protein interactions
594:Holliday junction resolvases
6412:Fructose 1,6-bisphosphatase
4468:Current Medicinal Chemistry
4433:Current Medicinal Chemistry
4327:10.1007/978-1-4614-7291-9_3
4191:10.1007/978-1-62703-670-2_7
4150:10.1016/j.virol.2015.02.031
1245:between the H2 complex and
1079:, leading to expression of
1075:, RNase H1 genes include a
7303:
5864:Prokaryotic DNA polymerase
5565:Minichromosome maintenance
5512:Origin recognition complex
4515:10.1016/j.bbrc.2007.12.014
4445:10.2174/092986710792065045
3948:Nature Reviews. Immunology
3058:10.1016/j.ajhg.2015.05.013
1836:Aicardi–Goutières syndrome
1659:phylogenetic relationships
1517:
1482:(AGS), which manifests as
1480:Aicardi–Goutières syndrome
491:Aicardi–Goutières syndrome
7137:Michaelis–Menten kinetics
6649:Galactosamine-6 sulfatase
6205:6-phosphogluconolactonase
5942:Eukaryotic DNA polymerase
5106:Itaya M (November 1990).
3727:10.1186/s13100-017-0087-y
3642:10.1038/s41594-018-0099-4
2531:Nature Structural Biology
1712:surface plasmon resonance
1520:Retroviral ribonuclease H
1171:
966:
503:retroviral ribonuclease H
367:
250:retroviral ribonuclease H
196:
37:
7029:Diffusion-limited enzyme
6397:Purple acid phosphatases
5361:Medical Subject Headings
5233:10.1073/pnas.95.22.12872
3908:British Medical Bulletin
3562:10.1021/acscatal.1c01493
3387:BMC Evolutionary Biology
1663:horizontal gene transfer
1249:, which localizes H2 to
779:centered on a conserved
647:gene encodes HI and the
5505:Pre-replication complex
5436:Pre-replication complex
5133:10.1073/pnas.87.21.8587
4775:10.1186/1472-6750-11-80
4105:10.1093/emboj/20.6.1449
3870:10.1074/jbc.M110.181974
3408:10.1186/1471-2148-7-128
3304:10.1126/science.1205016
2817:10.1074/jbc.M110.181974
2465:10.1126/science.1116702
2113:10.1126/science.1707186
1611:for the development of
816:TATA box binding domain
775:. All RNases H have an
6822:Microprocessor complex
6461:Beta-propeller phytase
5306:Nucleic Acids Research
5167:Ribonucleases - Part A
4954:10.1038/newbio234240a0
4542:Nucleic Acids Research
3687:10.1006/geno.2000.6488
3146:Nucleic Acids Research
2909:Nucleic Acids Research
2755:Nucleic Acids Research
2263:Nucleic Acids Research
2041:Nucleic Acids Research
1878:10.1006/jmbi.2001.5184
1740:ribonuclease inhibitor
1530:
1464:, a common feature of
1457:
1309:
760:
7122:Eadie–Hofstee diagram
7055:Allosteric regulation
6757:Endodeoxyribonuclease
6654:Iduronate-2-sulfatase
6407:Glucose 6-phosphatase
6193:Butyrylcholinesterase
5928:Replication protein A
5697:Origin of replication
3777:10.1093/molbev/msv008
2412:10.1038/emboj.2008.44
1789:reverse transcription
1724:RNase H-dependent PCR
1708:reverse transcription
1574:murine leukemia virus
1563:reverse transcriptase
1539:reverse transcription
1527:
1466:mitochondrial disease
1434:
1409:reverse transcriptase
1300:
820:reverse transcriptase
714:B. stearothermophilus
670:
586:retroviral integrases
507:reverse transcriptase
429:) is a family of non-
7132:Lineweaver–Burk plot
6940:Micrococcal nuclease
6775:Deoxyribonuclease IV
6770:Deoxyribonuclease II
6703:Exodeoxyribonuclease
6363:Alkaline phosphatase
6188:Acetylcholinesterase
5899:Replication factor C
4007:10.1002/ajmg.a.36887
1706:(cDNA) synthesis by
1602:long terminal repeat
1417:Long terminal repeat
526:mitochondrial genome
6795:UvrABC endonuclease
6765:Deoxyribonuclease I
6488:Protein phosphatase
6424:Protein phosphatase
6222:Bile salt-dependent
6210:PAF acetylhydrolase
5224:1998PNAS...9512872F
5124:1990PNAS...87.8587I
4981:Journal of Virology
4821:1969Sci...166..393S
4674:2015Ana...140.4566L
4144:. 479–480: 672–86.
3399:2007BMCEE...7..128K
3296:2011Sci...332.1561K
3208:10.1042/BST20140079
2868:10.7554/eLife.20533
2543:10.1038/nsb0497-298
2457:2005Sci...309.2057C
2362:2009JChPh.131w5101S
2275:10.1093/nar/gkt1414
2105:1991Sci...252...88D
1779:and in a sample of
1769:" to designate its
1629:mechanism of action
1592:of the RT protein.
7091:Enzyme superfamily
7024:Enzyme promiscuity
6928:Mung bean nuclease
6787:Restriction enzyme
6780:Restriction enzyme
5318:10.1093/nar/gkh209
4682:10.1039/C5AN00679A
4554:10.1093/nar/gkt045
4183:Human Retroviruses
3921:10.1093/bmb/ldn049
3461:10.1111/febs.12035
3158:10.1093/nar/gkn913
2921:10.1093/nar/gkw350
2767:10.1093/nar/gkq980
2053:10.1093/nar/gku615
1688:laboratory reagent
1661:, suggesting that
1580:activity produces
1531:
1458:
1310:
1302:Reaction mechanism
761:
604:proteins, various
7247:
7246:
6956:
6955:
6952:
6951:
6948:
6947:
6737:
6736:
6729:Oligonucleotidase
6674:deoxyribonuclease
6642:Steroid sulfatase
6517:Phosphodiesterase
6246:Hormone-sensitive
6118:
6117:
6075:
6074:
5911:Flap endonuclease
5741:
5740:
5728:Okazaki fragments
5184:978-0-12-182242-2
4762:BMC Biotechnology
4735:10.1021/ja039823p
4609:978-0-471-14272-0
4336:978-1-4614-7290-2
4236:10.1271/bbb.90777
4200:978-1-62703-669-6
3822:10.1159/000084971
3556:(13): 7915–7927.
3510:10.1021/ja411408x
3355:10.1021/bi982207z
3121:978-3-642-21077-8
2508:10.1021/bi982684h
2451:(5743): 2057–60.
2370:10.1063/1.3270167
1832:sequence identity
1735:Pyrococcus abyssi
1728:hyperthermophilic
1704:complementary DNA
1692:molecular biology
1559:hepatitis B virus
1553:examples include
1492:type I interferon
1282:sequence identity
1234:
1233:
1230:
1229:
1225:structure summary
1105:mitochondrial DNA
1046:Okazaki fragments
1029:
1028:
1025:
1024:
1020:structure summary
566:bonds to leave a
416:
415:
412:
411:
331:metabolic pathway
245:
244:
241:
240:
144:metabolic pathway
16:(Redirected from
7294:
7264:
7263:
7255:
7127:Hanes–Woolf plot
7070:Enzyme activator
7065:Enzyme inhibitor
7039:Enzyme catalysis
6983:
6976:
6969:
6960:
6805:Endoribonuclease
6791:
6785:
6753:
6699:
6685:
6385:Acid phosphatase
6266:Monoacylglycerol
6176:ester hydrolases
6145:
6138:
6131:
6122:
5868:DNA polymerase I
5752:
5712:Replication fork
5604:Licensing factor
5420:
5391:
5384:
5377:
5368:
5340:
5339:
5329:
5297:
5291:
5290:
5262:
5256:
5255:
5245:
5235:
5203:
5197:
5196:
5162:
5156:
5155:
5145:
5135:
5103:
5097:
5096:
5086:
5062:
5056:
5055:
5045:
5021:
5015:
5014:
5004:
4972:
4966:
4965:
4937:
4931:
4930:
4920:
4896:
4890:
4889:
4879:
4855:
4849:
4848:
4804:
4798:
4797:
4787:
4777:
4753:
4747:
4746:
4728:
4708:
4702:
4701:
4656:
4650:
4649:
4643:
4639:
4637:
4629:
4587:
4576:
4575:
4565:
4533:
4527:
4526:
4498:
4492:
4491:
4463:
4457:
4456:
4428:
4422:
4421:
4401:
4395:
4394:
4384:
4374:
4372:10.3390/v2040900
4350:
4341:
4340:
4314:
4305:
4304:
4294:
4277:(1–2): 186–202.
4262:
4256:
4255:
4219:
4213:
4212:
4178:
4172:
4171:
4161:
4133:
4127:
4126:
4116:
4093:The EMBO Journal
4084:
4078:
4077:
4067:
4035:
4029:
4028:
4018:
3986:
3980:
3979:
3943:
3934:
3933:
3923:
3899:
3893:
3892:
3882:
3872:
3863:(12): 10540–50.
3848:
3842:
3841:
3816:(1–4): 392–401.
3805:
3799:
3798:
3788:
3756:
3750:
3749:
3739:
3729:
3705:
3699:
3698:
3670:
3664:
3663:
3653:
3621:
3615:
3614:
3604:
3580:
3574:
3573:
3541:
3532:
3531:
3521:
3489:
3483:
3482:
3472:
3455:(24): 4492–500.
3440:
3431:
3430:
3420:
3410:
3378:
3367:
3366:
3337:
3326:
3325:
3315:
3290:(6037): 1561–4.
3275:
3269:
3268:
3258:
3226:
3220:
3219:
3191:
3180:
3179:
3169:
3137:
3126:
3125:
3101:
3091:
3080:
3079:
3069:
3037:
3028:
3027:
3017:
2993:
2987:
2986:
2976:
2952:
2943:
2942:
2932:
2915:(11): 5299–312.
2900:
2891:
2890:
2880:
2870:
2846:
2840:
2839:
2829:
2819:
2810:(12): 10540–50.
2795:
2789:
2788:
2778:
2746:
2740:
2739:
2711:
2705:
2704:
2694:
2670:
2661:
2660:
2650:
2627:The FEBS Journal
2618:
2612:
2611:
2601:
2569:
2563:
2562:
2526:
2520:
2519:
2491:
2485:
2484:
2440:
2434:
2433:
2423:
2400:The EMBO Journal
2391:
2382:
2381:
2345:
2339:
2338:
2306:
2297:
2296:
2286:
2254:
2245:
2244:
2213:The FEBS Journal
2208:
2177:
2176:
2166:
2143:The EMBO Journal
2134:
2125:
2124:
2088:
2075:
2074:
2064:
2032:
2021:
2020:
1983:
1972:
1971:
1961:
1938:The FEBS Journal
1929:
1890:
1889:
1861:
1851:
1716:Okazaki fragment
1698:preparations of
1547:dsDNA-RT viruses
1476:genetic disorder
1421:retrotransposons
1362:In human biology
1340:transition state
1251:replication foci
1173:
1119:
968:
902:
758:
742:
726:
710:
694:
630:Escherichia coli
444:the cleavage of
369:
247:
198:
42:
30:
21:
7302:
7301:
7297:
7296:
7295:
7293:
7292:
7291:
7272:
7271:
7270:
7258:
7250:
7248:
7243:
7155:Oxidoreductases
7141:
7117:Enzyme kinetics
7105:
7101:List of enzymes
7074:
7043:
7014:Catalytic triad
6992:
6987:
6957:
6944:
6911:
6799:
6789:
6783:
6746:
6733:
6721:Exoribonuclease
6715:
6692:
6676:
6672:
6663:
6637:Arylsulfatase L
6632:Arylsulfatase B
6627:Arylsulfatase A
6602:
6515:
6506:
6345:
6313:
6175:
6163:
6149:
6119:
6114:
6071:
6049:
5889:
5885:
5879:
5873:Klenow fragment
5756:
5737:
5721:leading strands
5685:
5495:
5491:
5485:
5424:
5409:
5398:DNA replication
5395:
5348:
5343:
5299:
5298:
5294:
5264:
5263:
5259:
5218:(22): 12872–7.
5205:
5204:
5200:
5185:
5164:
5163:
5159:
5118:(21): 8587–91.
5105:
5104:
5100:
5064:
5063:
5059:
5023:
5022:
5018:
4974:
4973:
4969:
4939:
4938:
4934:
4898:
4897:
4893:
4857:
4856:
4852:
4815:(3903): 393–5.
4806:
4805:
4801:
4755:
4754:
4750:
4726:10.1.1.475.1922
4710:
4709:
4705:
4668:(13): 4566–75.
4658:
4657:
4653:
4640:
4630:
4610:
4589:
4588:
4579:
4535:
4534:
4530:
4500:
4499:
4495:
4474:(17): 1956–67.
4465:
4464:
4460:
4439:(26): 2837–53.
4430:
4429:
4425:
4403:
4402:
4398:
4352:
4351:
4344:
4337:
4316:
4315:
4308:
4264:
4263:
4259:
4221:
4220:
4216:
4201:
4180:
4179:
4175:
4135:
4134:
4130:
4086:
4085:
4081:
4037:
4036:
4032:
3988:
3987:
3983:
3960:10.1038/nri3850
3945:
3944:
3937:
3901:
3900:
3896:
3850:
3849:
3845:
3807:
3806:
3802:
3771:(5): 1197–207.
3758:
3757:
3753:
3707:
3706:
3702:
3672:
3671:
3667:
3623:
3622:
3618:
3582:
3581:
3577:
3543:
3542:
3535:
3491:
3490:
3486:
3442:
3441:
3434:
3380:
3379:
3370:
3339:
3338:
3329:
3277:
3276:
3272:
3228:
3227:
3223:
3193:
3192:
3183:
3139:
3138:
3129:
3122:
3093:
3092:
3083:
3039:
3038:
3031:
2995:
2994:
2990:
2967:(10): 789–802.
2954:
2953:
2946:
2902:
2901:
2894:
2848:
2847:
2843:
2797:
2796:
2792:
2748:
2747:
2743:
2713:
2712:
2708:
2672:
2671:
2664:
2620:
2619:
2615:
2584:(1–2): 86–103.
2571:
2570:
2566:
2528:
2527:
2523:
2493:
2492:
2488:
2442:
2441:
2437:
2393:
2392:
2385:
2347:
2346:
2342:
2308:
2307:
2300:
2256:
2255:
2248:
2210:
2209:
2180:
2136:
2135:
2128:
2099:(5002): 88–95.
2090:
2089:
2078:
2047:(14): 9285–94.
2034:
2033:
2024:
1989:Nature Genetics
1985:
1984:
1975:
1944:(6): 1494–505.
1931:
1930:
1893:
1863:
1853:
1852:
1848:
1844:
1825:when the yeast
1817:homolog of the
1748:
1738:. Of note, the
1684:
1650:domains of life
1646:
1522:
1516:
1429:
1427:Role in disease
1364:
1295:
1117:
1115:Ribonuclease H2
1050:DNA replication
900:
898:Ribonuclease H1
853:
837:protein folding
750:
734:
718:
702:
686:
665:
538:
522:DNA replication
499:domains of life
51:
28:
23:
22:
15:
12:
11:
5:
7300:
7298:
7290:
7289:
7284:
7274:
7273:
7269:
7268:
7245:
7244:
7242:
7241:
7228:
7215:
7202:
7189:
7176:
7163:
7149:
7147:
7143:
7142:
7140:
7139:
7134:
7129:
7124:
7119:
7113:
7111:
7107:
7106:
7104:
7103:
7098:
7093:
7088:
7082:
7080:
7079:Classification
7076:
7075:
7073:
7072:
7067:
7062:
7057:
7051:
7049:
7045:
7044:
7042:
7041:
7036:
7031:
7026:
7021:
7016:
7011:
7006:
7000:
6998:
6994:
6993:
6988:
6986:
6985:
6978:
6971:
6963:
6954:
6953:
6950:
6949:
6946:
6945:
6943:
6942:
6937:
6932:
6931:
6930:
6919:
6917:
6913:
6912:
6910:
6909:
6904:
6903:
6902:
6897:
6892:
6887:
6877:
6872:
6867:
6862:
6861:
6860:
6855:
6850:
6845:
6835:
6834:
6833:
6824:
6809:
6807:
6801:
6800:
6798:
6797:
6792:
6777:
6772:
6767:
6761:
6759:
6750:
6739:
6738:
6735:
6734:
6732:
6731:
6725:
6723:
6717:
6716:
6714:
6713:
6707:
6705:
6696:
6682:
6665:
6664:
6662:
6661:
6656:
6651:
6646:
6645:
6644:
6639:
6634:
6629:
6616:
6614:
6604:
6603:
6601:
6600:
6595:
6585:
6580:
6571:
6566:
6561:
6556:
6555:
6554:
6544:
6543:
6542:
6537:
6527:
6521:
6519:
6508:
6507:
6505:
6504:
6499:
6494:
6485:
6484:
6483:
6465:
6464:
6463:
6453:
6448:
6443:
6438:
6433:
6432:
6431:
6421:
6420:
6419:
6409:
6404:
6399:
6382:
6381:
6380:
6375:
6370:
6359:
6357:
6347:
6346:
6344:
6343:
6338:
6333:
6327:
6325:
6315:
6314:
6312:
6311:
6306:
6300:
6299:
6298:
6297:
6292:
6287:
6276:
6275:
6274:
6273:
6271:Diacylglycerol
6268:
6263:
6258:
6253:
6248:
6243:
6238:
6233:
6224:
6213:
6212:
6207:
6202:
6200:Pectinesterase
6197:
6196:
6195:
6190:
6183:Cholinesterase
6179:
6177:
6165:
6164:
6150:
6148:
6147:
6140:
6133:
6125:
6116:
6115:
6113:
6112:
6111:
6110:
6105:
6100:
6085:
6083:
6077:
6076:
6073:
6072:
6070:
6069:
6064:
6057:
6055:
6051:
6050:
6048:
6047:
6041:
6040:
6039:
6038:
6027:
6026:
6025:
6024:
6019:
6014:
6009:
5999:
5998:
5997:
5992:
5987:
5982:
5972:
5971:
5970:
5965:
5960:
5955:
5945:
5938:
5937:
5936:
5935:
5925:
5920:
5919:
5918:
5908:
5907:
5906:
5895:
5893:
5881:
5880:
5878:
5877:
5876:
5875:
5860:
5859:
5858:
5857:
5847:
5842:
5837:
5832:
5831:
5830:
5825:
5820:
5815:
5810:
5805:
5800:
5795:
5790:
5785:
5780:
5775:
5764:
5762:
5749:
5743:
5742:
5739:
5738:
5736:
5735:
5730:
5725:
5724:
5723:
5708:
5707:
5693:
5691:
5687:
5686:
5684:
5683:
5678:
5668:
5667:
5657:
5656:
5655:
5654:
5649:
5638:
5637:
5636:
5635:
5630:
5625:
5614:
5613:
5607:
5606:
5600:
5599:
5598:
5597:
5592:
5587:
5582:
5577:
5572:
5561:
5560:
5554:
5553:
5547:
5546:
5545:
5544:
5539:
5534:
5529:
5524:
5519:
5508:
5507:
5501:
5499:
5494:preparation in
5487:
5486:
5484:
5483:
5482:
5481:
5470:
5469:
5468:
5467:
5462:
5457:
5446:
5445:
5439:
5438:
5432:
5430:
5417:
5411:
5410:
5396:
5394:
5393:
5386:
5379:
5371:
5365:
5364:
5354:
5347:
5346:External links
5344:
5342:
5341:
5292:
5257:
5198:
5183:
5157:
5098:
5077:(2): 1276–81.
5057:
5016:
4987:(6): 1136–42.
4967:
4932:
4891:
4850:
4799:
4748:
4719:(13): 4086–7.
4703:
4651:
4642:|journal=
4608:
4577:
4548:(5): 2832–45.
4528:
4493:
4458:
4423:
4396:
4342:
4335:
4306:
4271:Virus Research
4257:
4214:
4199:
4173:
4128:
4099:(6): 1449–61.
4079:
4056:10.1086/521373
4030:
4001:(2): 296–312.
3981:
3935:
3894:
3843:
3800:
3751:
3700:
3665:
3636:(8): 715–721.
3616:
3575:
3533:
3504:(8): 3137–44.
3484:
3432:
3368:
3327:
3270:
3235:Molecular Cell
3221:
3181:
3127:
3120:
3081:
3029:
3002:Molecular Cell
2988:
2961:Genes to Cells
2944:
2892:
2841:
2790:
2761:(9): 3652–66.
2741:
2706:
2679:Molecular Cell
2662:
2633:(6): 1506–16.
2613:
2578:Virus Research
2564:
2537:(4): 298–304.
2521:
2502:(12): 3831–6.
2486:
2435:
2406:(7): 1172–81.
2383:
2356:(23): 235101.
2340:
2298:
2269:(7): 4160–79.
2246:
2219:(6): 1482–93.
2178:
2126:
2076:
2022:
2001:10.1038/ng1842
1973:
1891:
1845:
1843:
1840:
1823:bioinformatics
1747:
1744:
1683:
1680:
1645:
1642:
1613:antiretroviral
1533:Two groups of
1515:
1512:
1488:dermatological
1428:
1425:
1397:
1396:
1390:
1384:
1378:
1363:
1360:
1308:RNase H domain
1294:
1291:
1232:
1231:
1228:
1227:
1222:
1216:
1215:
1202:
1196:
1195:
1185:
1178:
1177:
1169:
1168:
1163:
1157:
1156:
1151:
1144:
1143:
1138:
1132:
1131:
1128:
1124:
1123:
1116:
1113:
1093:knockout mouse
1033:ribonucleotide
1027:
1026:
1023:
1022:
1017:
1011:
1010:
997:
991:
990:
980:
973:
972:
964:
963:
958:
952:
951:
946:
940:
939:
934:
927:
926:
921:
915:
914:
911:
907:
906:
899:
896:
857:phosphodiester
852:
849:
781:sequence motif
664:
661:
564:phosphodiester
547:with a shared
537:
534:
419:Ribonuclease H
414:
413:
410:
409:
404:
398:
397:
392:
386:
385:
380:
374:
373:
365:
364:
353:
346:
345:
340:
334:
333:
328:
322:
321:
316:
310:
309:
304:
298:
297:
292:
286:
285:
280:
274:
273:
269:
268:
263:
257:
256:
252:
251:
243:
242:
239:
238:
233:
227:
226:
221:
215:
214:
209:
203:
202:
194:
193:
184:
178:
177:
166:
159:
158:
153:
147:
146:
141:
135:
134:
129:
123:
122:
117:
111:
110:
105:
99:
98:
93:
87:
86:
82:
81:
76:
70:
69:
64:
58:
57:
53:
52:
43:
35:
34:
33:ribonuclease H
26:
24:
14:
13:
10:
9:
6:
4:
3:
2:
7299:
7288:
7285:
7283:
7282:Ribonucleases
7280:
7279:
7277:
7267:
7262:
7257:
7253:
7239:
7235:
7234:
7229:
7226:
7222:
7221:
7216:
7213:
7209:
7208:
7203:
7200:
7196:
7195:
7190:
7187:
7183:
7182:
7177:
7174:
7170:
7169:
7164:
7161:
7157:
7156:
7151:
7150:
7148:
7144:
7138:
7135:
7133:
7130:
7128:
7125:
7123:
7120:
7118:
7115:
7114:
7112:
7108:
7102:
7099:
7097:
7096:Enzyme family
7094:
7092:
7089:
7087:
7084:
7083:
7081:
7077:
7071:
7068:
7066:
7063:
7061:
7060:Cooperativity
7058:
7056:
7053:
7052:
7050:
7046:
7040:
7037:
7035:
7032:
7030:
7027:
7025:
7022:
7020:
7019:Oxyanion hole
7017:
7015:
7012:
7010:
7007:
7005:
7002:
7001:
6999:
6995:
6991:
6984:
6979:
6977:
6972:
6970:
6965:
6964:
6961:
6941:
6938:
6936:
6933:
6929:
6926:
6925:
6924:
6921:
6920:
6918:
6914:
6908:
6905:
6901:
6898:
6896:
6893:
6891:
6888:
6886:
6883:
6882:
6881:
6878:
6876:
6873:
6871:
6868:
6866:
6863:
6859:
6856:
6854:
6851:
6849:
6846:
6844:
6841:
6840:
6839:
6836:
6832:
6828:
6825:
6823:
6819:
6816:
6815:
6814:
6811:
6810:
6808:
6806:
6802:
6796:
6793:
6788:
6781:
6778:
6776:
6773:
6771:
6768:
6766:
6763:
6762:
6760:
6758:
6754:
6751:
6749:
6744:
6740:
6730:
6727:
6726:
6724:
6722:
6718:
6712:
6709:
6708:
6706:
6704:
6700:
6697:
6695:
6690:
6686:
6683:
6680:
6675:
6670:
6666:
6660:
6657:
6655:
6652:
6650:
6647:
6643:
6640:
6638:
6635:
6633:
6630:
6628:
6625:
6624:
6623:
6622:
6621:arylsulfatase
6618:
6617:
6615:
6613:
6609:
6605:
6599:
6596:
6593:
6589:
6586:
6584:
6581:
6579:
6575:
6572:
6570:
6567:
6565:
6562:
6560:
6557:
6553:
6550:
6549:
6548:
6545:
6541:
6538:
6536:
6533:
6532:
6531:
6530:Phospholipase
6528:
6526:
6523:
6522:
6520:
6518:
6513:
6509:
6503:
6500:
6498:
6495:
6493:
6489:
6486:
6482:
6478:
6474:
6471:
6470:
6469:
6466:
6462:
6459:
6458:
6457:
6454:
6452:
6449:
6447:
6444:
6442:
6439:
6437:
6434:
6430:
6427:
6426:
6425:
6422:
6418:
6415:
6414:
6413:
6410:
6408:
6405:
6403:
6400:
6398:
6394:
6390:
6386:
6383:
6379:
6376:
6374:
6371:
6369:
6366:
6365:
6364:
6361:
6360:
6358:
6356:
6352:
6348:
6342:
6339:
6337:
6334:
6332:
6329:
6328:
6326:
6324:
6320:
6316:
6310:
6307:
6305:
6302:
6301:
6296:
6293:
6291:
6288:
6286:
6283:
6282:
6281:
6280:Phospholipase
6278:
6277:
6272:
6269:
6267:
6264:
6262:
6259:
6257:
6254:
6252:
6249:
6247:
6244:
6242:
6239:
6237:
6234:
6232:
6228:
6225:
6223:
6220:
6219:
6218:
6215:
6214:
6211:
6208:
6206:
6203:
6201:
6198:
6194:
6191:
6189:
6186:
6185:
6184:
6181:
6180:
6178:
6174:
6170:
6166:
6161:
6157:
6153:
6146:
6141:
6139:
6134:
6132:
6127:
6126:
6123:
6109:
6106:
6104:
6101:
6099:
6096:
6095:
6094:
6090:
6087:
6086:
6084:
6082:
6078:
6068:
6065:
6063:
6059:
6058:
6056:
6052:
6046:
6043:
6042:
6037:
6034:
6033:
6032:
6029:
6028:
6023:
6020:
6018:
6015:
6013:
6010:
6008:
6005:
6004:
6003:
6000:
5996:
5993:
5991:
5988:
5986:
5983:
5981:
5978:
5977:
5976:
5973:
5969:
5966:
5964:
5961:
5959:
5956:
5954:
5951:
5950:
5949:
5946:
5943:
5940:
5939:
5934:
5931:
5930:
5929:
5926:
5924:
5923:Topoisomerase
5921:
5917:
5914:
5913:
5912:
5909:
5905:
5902:
5901:
5900:
5897:
5896:
5894:
5891:
5882:
5874:
5871:
5870:
5869:
5865:
5862:
5861:
5856:
5853:
5852:
5851:
5850:Topoisomerase
5848:
5846:
5843:
5841:
5838:
5836:
5833:
5829:
5826:
5824:
5821:
5819:
5816:
5814:
5811:
5809:
5806:
5804:
5801:
5799:
5796:
5794:
5791:
5789:
5786:
5784:
5781:
5779:
5776:
5774:
5771:
5770:
5769:
5766:
5765:
5763:
5760:
5753:
5750:
5748:
5744:
5734:
5731:
5729:
5726:
5722:
5718:
5715:
5714:
5713:
5710:
5709:
5706:
5702:
5698:
5695:
5694:
5692:
5688:
5682:
5679:
5677:
5673:
5670:
5669:
5666:
5662:
5659:
5658:
5653:
5650:
5648:
5645:
5644:
5643:
5640:
5639:
5634:
5631:
5629:
5626:
5624:
5621:
5620:
5619:
5616:
5615:
5612:
5609:
5608:
5605:
5602:
5601:
5596:
5593:
5591:
5588:
5586:
5583:
5581:
5578:
5576:
5573:
5571:
5568:
5567:
5566:
5563:
5562:
5559:
5556:
5555:
5552:
5549:
5548:
5543:
5540:
5538:
5535:
5533:
5530:
5528:
5525:
5523:
5520:
5518:
5515:
5514:
5513:
5510:
5509:
5506:
5503:
5502:
5500:
5497:
5488:
5480:
5477:
5476:
5475:
5472:
5471:
5466:
5463:
5461:
5458:
5456:
5453:
5452:
5451:
5448:
5447:
5444:
5441:
5440:
5437:
5434:
5433:
5431:
5428:
5421:
5418:
5416:
5412:
5407:
5403:
5399:
5392:
5387:
5385:
5380:
5378:
5373:
5372:
5369:
5362:
5358:
5355:
5353:
5350:
5349:
5345:
5337:
5333:
5328:
5323:
5319:
5315:
5312:(2): 407–14.
5311:
5307:
5303:
5296:
5293:
5288:
5284:
5280:
5276:
5272:
5268:
5261:
5258:
5253:
5249:
5244:
5239:
5234:
5229:
5225:
5221:
5217:
5213:
5209:
5202:
5199:
5194:
5190:
5186:
5180:
5176:
5172:
5168:
5161:
5158:
5153:
5149:
5144:
5139:
5134:
5129:
5125:
5121:
5117:
5113:
5109:
5102:
5099:
5094:
5090:
5085:
5080:
5076:
5072:
5068:
5061:
5058:
5053:
5049:
5044:
5039:
5036:(1): 179–90.
5035:
5031:
5027:
5020:
5017:
5012:
5008:
5003:
4998:
4994:
4990:
4986:
4982:
4978:
4971:
4968:
4963:
4959:
4955:
4951:
4948:(51): 240–3.
4947:
4943:
4936:
4933:
4928:
4924:
4919:
4914:
4911:(7): 2621–4.
4910:
4906:
4902:
4895:
4892:
4887:
4883:
4878:
4873:
4870:(2): 278–83.
4869:
4865:
4861:
4854:
4851:
4846:
4842:
4838:
4834:
4830:
4826:
4822:
4818:
4814:
4810:
4803:
4800:
4795:
4791:
4786:
4781:
4776:
4771:
4767:
4763:
4759:
4752:
4749:
4744:
4740:
4736:
4732:
4727:
4722:
4718:
4714:
4707:
4704:
4699:
4695:
4691:
4687:
4683:
4679:
4675:
4671:
4667:
4663:
4655:
4652:
4647:
4635:
4627:
4623:
4619:
4615:
4611:
4605:
4601:
4597:
4593:
4592:Ribonucleases
4586:
4584:
4582:
4578:
4573:
4569:
4564:
4559:
4555:
4551:
4547:
4543:
4539:
4532:
4529:
4524:
4520:
4516:
4512:
4509:(3): 607–11.
4508:
4504:
4497:
4494:
4489:
4485:
4481:
4477:
4473:
4469:
4462:
4459:
4454:
4450:
4446:
4442:
4438:
4434:
4427:
4424:
4419:
4415:
4412:(4): 183–94.
4411:
4407:
4400:
4397:
4392:
4388:
4383:
4378:
4373:
4368:
4365:(4): 900–26.
4364:
4360:
4356:
4349:
4347:
4343:
4338:
4332:
4328:
4324:
4320:
4313:
4311:
4307:
4302:
4298:
4293:
4288:
4284:
4280:
4276:
4272:
4268:
4261:
4258:
4253:
4249:
4245:
4241:
4237:
4233:
4229:
4225:
4218:
4215:
4210:
4206:
4202:
4196:
4192:
4188:
4184:
4177:
4174:
4169:
4165:
4160:
4155:
4151:
4147:
4143:
4139:
4132:
4129:
4124:
4120:
4115:
4110:
4106:
4102:
4098:
4094:
4090:
4083:
4080:
4075:
4071:
4066:
4061:
4057:
4053:
4050:(4): 713–25.
4049:
4045:
4041:
4034:
4031:
4026:
4022:
4017:
4012:
4008:
4004:
4000:
3996:
3992:
3985:
3982:
3977:
3973:
3969:
3965:
3961:
3957:
3954:(7): 429–40.
3953:
3949:
3942:
3940:
3936:
3931:
3927:
3922:
3917:
3913:
3909:
3905:
3898:
3895:
3890:
3886:
3881:
3876:
3871:
3866:
3862:
3858:
3854:
3847:
3844:
3839:
3835:
3831:
3827:
3823:
3819:
3815:
3811:
3804:
3801:
3796:
3792:
3787:
3782:
3778:
3774:
3770:
3766:
3762:
3755:
3752:
3747:
3743:
3738:
3733:
3728:
3723:
3719:
3715:
3711:
3704:
3701:
3696:
3692:
3688:
3684:
3681:(3): 314–20.
3680:
3676:
3669:
3666:
3661:
3657:
3652:
3647:
3643:
3639:
3635:
3631:
3627:
3620:
3617:
3612:
3608:
3603:
3598:
3595:(1): 143–54.
3594:
3590:
3589:Mol Microbiol
3586:
3579:
3576:
3571:
3567:
3563:
3559:
3555:
3551:
3550:ACS Catalysis
3547:
3540:
3538:
3534:
3529:
3525:
3520:
3515:
3511:
3507:
3503:
3499:
3495:
3488:
3485:
3480:
3476:
3471:
3466:
3462:
3458:
3454:
3450:
3446:
3439:
3437:
3433:
3428:
3424:
3419:
3414:
3409:
3404:
3400:
3396:
3392:
3388:
3384:
3377:
3375:
3373:
3369:
3364:
3360:
3356:
3352:
3349:(2): 605–18.
3348:
3344:
3336:
3334:
3332:
3328:
3323:
3319:
3314:
3309:
3305:
3301:
3297:
3293:
3289:
3285:
3281:
3274:
3271:
3266:
3262:
3257:
3252:
3248:
3244:
3241:(6): 978–88.
3240:
3236:
3232:
3225:
3222:
3217:
3213:
3209:
3205:
3202:(4): 717–25.
3201:
3197:
3190:
3188:
3186:
3182:
3177:
3173:
3168:
3163:
3159:
3155:
3152:(1): 96–110.
3151:
3147:
3143:
3136:
3134:
3132:
3128:
3123:
3117:
3113:
3109:
3105:
3100:
3099:
3098:Ribonucleases
3090:
3088:
3086:
3082:
3077:
3073:
3068:
3063:
3059:
3055:
3052:(1): 186–93.
3051:
3047:
3043:
3036:
3034:
3030:
3025:
3021:
3016:
3011:
3008:(3): 807–15.
3007:
3003:
2999:
2992:
2989:
2984:
2980:
2975:
2970:
2966:
2962:
2958:
2951:
2949:
2945:
2940:
2936:
2931:
2926:
2922:
2918:
2914:
2910:
2906:
2899:
2897:
2893:
2888:
2884:
2879:
2874:
2869:
2864:
2860:
2856:
2852:
2845:
2842:
2837:
2833:
2828:
2823:
2818:
2813:
2809:
2805:
2801:
2794:
2791:
2786:
2782:
2777:
2772:
2768:
2764:
2760:
2756:
2752:
2745:
2742:
2737:
2733:
2729:
2725:
2721:
2717:
2710:
2707:
2702:
2698:
2693:
2688:
2684:
2680:
2676:
2669:
2667:
2663:
2658:
2654:
2649:
2644:
2640:
2636:
2632:
2628:
2624:
2617:
2614:
2609:
2605:
2600:
2595:
2591:
2587:
2583:
2579:
2575:
2568:
2565:
2560:
2556:
2552:
2548:
2544:
2540:
2536:
2532:
2525:
2522:
2517:
2513:
2509:
2505:
2501:
2497:
2490:
2487:
2482:
2478:
2474:
2470:
2466:
2462:
2458:
2454:
2450:
2446:
2439:
2436:
2431:
2427:
2422:
2417:
2413:
2409:
2405:
2401:
2397:
2390:
2388:
2384:
2379:
2375:
2371:
2367:
2363:
2359:
2355:
2351:
2344:
2341:
2336:
2332:
2328:
2324:
2320:
2316:
2312:
2305:
2303:
2299:
2294:
2290:
2285:
2280:
2276:
2272:
2268:
2264:
2260:
2253:
2251:
2247:
2242:
2238:
2234:
2230:
2226:
2222:
2218:
2214:
2207:
2205:
2203:
2201:
2199:
2197:
2195:
2193:
2191:
2189:
2187:
2185:
2183:
2179:
2174:
2170:
2165:
2160:
2156:
2152:
2149:(1): 239–43.
2148:
2144:
2140:
2133:
2131:
2127:
2122:
2118:
2114:
2110:
2106:
2102:
2098:
2094:
2087:
2085:
2083:
2081:
2077:
2072:
2068:
2063:
2058:
2054:
2050:
2046:
2042:
2038:
2031:
2029:
2027:
2023:
2018:
2014:
2010:
2006:
2002:
1998:
1994:
1990:
1982:
1980:
1978:
1974:
1969:
1965:
1960:
1955:
1951:
1947:
1943:
1939:
1935:
1928:
1926:
1924:
1922:
1920:
1918:
1916:
1914:
1912:
1910:
1908:
1906:
1904:
1902:
1900:
1898:
1896:
1892:
1887:
1883:
1879:
1875:
1872:(4): 863–71.
1871:
1867:
1860:
1856:
1850:
1847:
1841:
1839:
1837:
1833:
1828:
1824:
1820:
1816:
1815:
1814:S. cerevisiae
1810:
1806:
1801:
1798:
1794:
1790:
1786:
1782:
1778:
1777:
1772:
1768:
1764:
1761:
1757:
1753:
1745:
1743:
1741:
1737:
1736:
1732:
1729:
1725:
1721:
1720:hot start PCR
1717:
1713:
1709:
1705:
1701:
1697:
1693:
1689:
1681:
1679:
1675:
1673:
1669:
1664:
1660:
1655:
1651:
1643:
1641:
1638:
1634:
1630:
1626:
1622:
1618:
1614:
1610:
1605:
1603:
1598:
1593:
1591:
1587:
1583:
1579:
1575:
1571:
1566:
1564:
1560:
1556:
1552:
1548:
1544:
1540:
1536:
1526:
1521:
1513:
1511:
1509:
1505:
1501:
1497:
1493:
1489:
1485:
1481:
1477:
1474:
1469:
1467:
1463:
1455:
1451:
1447:
1443:
1439:
1433:
1426:
1424:
1422:
1418:
1414:
1410:
1406:
1402:
1394:
1391:
1388:
1385:
1382:
1379:
1376:
1373:
1372:
1371:
1369:
1361:
1359:
1355:
1353:
1349:
1345:
1341:
1336:
1334:
1330:
1326:
1321:
1319:
1315:
1307:
1303:
1299:
1292:
1290:
1288:
1283:
1278:
1276:
1272:
1268:
1264:
1260:
1254:
1252:
1248:
1244:
1240:
1226:
1223:
1221:
1217:
1214:
1210:
1206:
1203:
1201:
1197:
1193:
1189:
1186:
1183:
1179:
1174:
1170:
1167:
1164:
1162:
1158:
1155:
1152:
1149:
1145:
1142:
1139:
1137:
1133:
1129:
1125:
1120:
1114:
1112:
1110:
1106:
1102:
1101:embryogenesis
1098:
1094:
1090:
1086:
1082:
1078:
1074:
1069:
1067:
1066:
1065:S. cerevisiae
1061:
1057:
1056:
1051:
1047:
1043:
1038:
1034:
1021:
1018:
1016:
1012:
1009:
1005:
1001:
998:
996:
992:
988:
984:
981:
978:
974:
969:
965:
962:
959:
957:
953:
950:
947:
945:
941:
938:
935:
932:
928:
925:
922:
920:
916:
912:
908:
903:
897:
895:
893:
889:
885:
881:
876:
873:
869:
866:
862:
858:
850:
848:
846:
842:
838:
834:
833:model systems
830:
829:
823:
821:
817:
813:
812:heterotrimers
809:
805:
801:
796:
794:
790:
786:
782:
778:
774:
770:
766:
757:
753:
748:
747:
741:
737:
732:
731:
725:
721:
716:
715:
709:
705:
700:
699:
693:
689:
684:
683:
678:
674:
669:
662:
660:
658:
654:
650:
646:
642:
639:RNase H1. In
638:
637:
632:
631:
626:
622:
617:
615:
611:
607:
603:
599:
595:
591:
587:
583:
579:
576:
572:
569:
565:
561:
558:
554:
550:
546:
543:
535:
533:
531:
527:
523:
518:
516:
512:
508:
504:
500:
496:
492:
488:
484:
480:
475:
473:
469:
465:
461:
458:
454:
451:
447:
443:
439:
436:
432:
428:
424:
421:(abbreviated
420:
408:
405:
403:
399:
396:
393:
391:
387:
384:
381:
379:
375:
370:
366:
363:
360:
357:
354:
351:
347:
344:
341:
339:
335:
332:
329:
327:
323:
320:
317:
315:
311:
308:
307:NiceZyme view
305:
303:
299:
296:
293:
291:
287:
284:
281:
279:
275:
270:
267:
264:
262:
258:
253:
248:
237:
234:
232:
228:
225:
222:
220:
216:
213:
210:
208:
204:
199:
195:
192:
188:
185:
183:
182:Gene Ontology
179:
176:
173:
170:
167:
164:
160:
157:
154:
152:
148:
145:
142:
140:
136:
133:
130:
128:
124:
121:
120:NiceZyme view
118:
116:
112:
109:
106:
104:
100:
97:
94:
92:
88:
83:
80:
77:
75:
71:
68:
65:
63:
59:
54:
49:
48:
41:
36:
31:
27:Enzyme family
19:
7233:Translocases
7230:
7217:
7204:
7191:
7178:
7168:Transferases
7165:
7152:
7009:Binding site
6790:}}
6784:{{
6748:Endonuclease
6679:ribonuclease
6619:
6402:Nucleotidase
6323:Thioesterase
6062:Processivity
5888:synthesis in
5309:
5305:
5295:
5270:
5267:FEBS Letters
5266:
5260:
5215:
5211:
5201:
5166:
5160:
5115:
5111:
5101:
5074:
5070:
5060:
5033:
5029:
5019:
4984:
4980:
4970:
4945:
4941:
4935:
4908:
4904:
4894:
4867:
4863:
4853:
4812:
4808:
4802:
4765:
4761:
4751:
4716:
4712:
4706:
4665:
4661:
4654:
4591:
4545:
4541:
4531:
4506:
4502:
4496:
4471:
4467:
4461:
4436:
4432:
4426:
4409:
4406:AIDS Reviews
4405:
4399:
4362:
4358:
4318:
4274:
4270:
4260:
4230:(2): 440–2.
4227:
4223:
4217:
4182:
4176:
4141:
4131:
4096:
4092:
4082:
4047:
4043:
4033:
3998:
3994:
3984:
3951:
3947:
3911:
3907:
3897:
3860:
3856:
3846:
3813:
3809:
3803:
3768:
3764:
3754:
3717:
3713:
3703:
3678:
3674:
3668:
3633:
3629:
3619:
3592:
3588:
3578:
3553:
3549:
3501:
3497:
3487:
3452:
3449:FEBS Journal
3448:
3390:
3386:
3346:
3343:Biochemistry
3342:
3287:
3283:
3273:
3238:
3234:
3224:
3199:
3195:
3149:
3145:
3097:
3049:
3045:
3005:
3001:
2991:
2964:
2960:
2912:
2908:
2858:
2854:
2844:
2807:
2803:
2793:
2758:
2754:
2744:
2719:
2715:
2709:
2682:
2678:
2630:
2626:
2616:
2581:
2577:
2567:
2534:
2530:
2524:
2499:
2496:Biochemistry
2495:
2489:
2448:
2444:
2438:
2403:
2399:
2353:
2349:
2343:
2321:(1): 76–83.
2318:
2314:
2266:
2262:
2216:
2212:
2146:
2142:
2096:
2092:
2044:
2040:
1995:(8): 910–6.
1992:
1988:
1941:
1937:
1869:
1865:
1849:
1818:
1812:
1808:
1805:purification
1802:
1796:
1792:
1774:
1770:
1766:
1758:activity in
1756:endonuclease
1752:Peter Hausen
1749:
1733:
1699:
1685:
1682:Applications
1676:
1647:
1606:
1594:
1582:minus-strand
1567:
1543:retroviruses
1532:
1484:neurological
1470:
1459:
1449:
1398:
1368:human genome
1365:
1356:
1337:
1322:
1311:
1279:
1275:cell nucleus
1259:processivity
1255:
1235:
1111:processing.
1085:mitochondria
1070:
1063:
1053:
1035:-containing
1030:
854:
844:
831:homolog, as
826:
824:
808:processivity
797:
783:composed of
762:
744:
728:
712:
696:
680:
676:
672:
648:
644:
640:
636:Homo sapiens
634:
628:
618:
610:spliceosomal
606:exonucleases
590:transposases
542:endonuclease
539:
532:structures.
519:
511:retroviruses
487:rare disease
483:human genome
476:
435:endonuclease
426:
422:
418:
417:
295:BRENDA entry
108:BRENDA entry
45:
7004:Active site
6923:Nuclease S1
6694:Exonuclease
6588:Lecithinase
6417:Calcineurin
6355:Phosphatase
6261:Lipoprotein
6251:Endothelial
6081:Termination
5755:Prokaryotic
5747:Replication
5423:Prokaryotic
5402:prokaryotic
5400:(comparing
5273:(1): 23–6.
4662:The Analyst
3914:: 183–201.
2722:(1): 12–9.
2685:(1): 5–13.
1785:RNA genomes
1781:oncoviruses
1722:, known as
1609:drug target
1438:active site
1314:active site
1122:Identifiers
1058:, RNase H1
1042:RNA primers
905:Identifiers
777:active site
698:T. maritima
627:. Thus the
625:prokaryotes
495:prokaryotes
283:IntEnz view
255:Identifiers
96:IntEnz view
56:Identifiers
7276:Categories
7207:Isomerases
7181:Hydrolases
7048:Regulation
6236:Pancreatic
6173:Carboxylic
6093:Telomerase
6067:DNA ligase
6060:Movement:
5884:Eukaryotic
5855:DNA gyrase
5840:DNA ligase
5759:elongation
5490:Eukaryotic
5427:initiation
5415:Initiation
5406:eukaryotic
3714:Mobile DNA
3393:(1): 128.
2861:: e20533.
1842:References
1625:chemotypes
1621:Inhibitors
1590:C-terminus
1551:Pathogenic
1518:See also:
1514:In viruses
1401:retroviral
1327:ions, but
1188:structures
1037:base pairs
983:structures
804:N-terminus
746:H. sapiens
730:H. sapiens
677:H. sapiens
621:eukaryotes
608:, and the
472:eukaryotes
457:hydrolytic
448:in an RNA/
433:-specific
352:structures
319:KEGG entry
165:structures
132:KEGG entry
79:9050-76-4
7287:EC 3.1.26
7086:EC number
6813:RNase III
6671:(includes
6612:Sulfatase
6525:Autotaxin
6389:Prostatic
6241:Lysosomal
6156:esterases
6152:Hydrolase
6031:DNA clamp
5845:DNA clamp
5835:Replisome
4721:CiteSeerX
4644:ignored (
4634:cite book
4626:221604377
3570:236285134
1862:;
1644:Evolution
1633:chelation
1631:based on
1478:known as
1446:threonine
1329:manganese
1325:magnesium
1318:histidine
1293:Mechanism
1166:IPR024567
1130:RNase HII
1060:knockouts
949:IPR002156
884:essential
880:substrate
875:phosphate
859:bonds of
835:to study
793:magnesium
789:glutamate
785:aspartate
773:α-helices
765:structure
743:;
727:;
711:;
695:;
663:Structure
602:Argonaute
582:nucleases
578:phosphate
549:substrate
489:known as
479:substrate
460:mechanism
453:substrate
272:Databases
266:3.1.26.13
85:Databases
50:RNase HI.
7110:Kinetics
7034:Cofactor
6997:Activity
6907:RNase T1
6669:Nuclease
6304:Cutinase
6089:Telomere
5705:Replicon
5661:Helicase
5652:RNASEH2A
5496:G1 phase
5450:Helicase
5336:14734815
5193:11582793
4845:43683241
4794:21831278
4743:15053580
4698:28974459
4690:26000345
4618:18972385
4572:23376926
4523:18073136
4488:24438523
4453:20858167
4418:12555693
4391:21994660
4301:18294720
4252:28110533
4244:20139597
4209:24158815
4168:25759099
4142:Virology
4123:11250910
4074:17846997
4025:25604658
3976:34259643
3968:26052098
3930:19129251
3889:21177858
3830:16093691
3795:25605791
3746:28293305
3720:(1): 4.
3695:11401447
3675:Genomics
3660:30076410
3611:18047582
3528:24499076
3479:23078533
3427:17663799
3322:21700875
3265:22195970
3216:25109948
3176:19015152
3076:26094573
3024:12667461
2983:11029655
2939:27131367
2887:27938663
2836:21177858
2785:21245041
2736:16232566
2701:16600865
2657:19228195
2608:18261820
2559:33673059
2516:10090773
2481:43823877
2473:16179479
2430:18337749
2378:20025349
2293:24464998
2241:29008571
2233:19228197
2071:25016521
2009:16845400
1968:19228196
1886:11734003
1731:archaeon
1696:Purified
1668:bacteria
1654:nuclease
1617:HIV/AIDS
1450:in vitro
1393:RNASEH2C
1387:RNASEH2B
1381:RNASEH2A
1239:sequence
1205:RCSB PDB
1161:InterPro
1087:and the
1081:isoforms
1000:RCSB PDB
944:InterPro
868:hydroxyl
851:Function
759:.
653:bacteria
612:protein
571:hydroxyl
560:duplexes
513:such as
464:bacteria
442:catalyze
431:sequence
407:proteins
395:articles
383:articles
356:RCSB PDB
236:proteins
224:articles
212:articles
169:RCSB PDB
67:3.1.26.4
7266:Biology
7220:Ligases
6990:Enzymes
6880:RNase E
6875:RNase Z
6870:RNase A
6865:RNase P
6838:RNase H
6456:Phytase
6256:Hepatic
6231:Lingual
6227:Gastric
6002:epsilon
5890:S phase
5717:Lagging
5672:Primase
5647:RNASEH1
5642:RNase H
5474:Primase
5357:RNase+H
5287:9462832
5252:9789007
5220:Bibcode
5152:2172991
5120:Bibcode
5093:6296074
5011:4118867
4962:4331605
4927:4572736
4886:5506170
4837:5812039
4817:Bibcode
4809:Science
4785:3224242
4670:Bibcode
4563:3597702
4382:3185654
4359:Viruses
4292:2443788
4159:4424072
4065:2227922
4016:4382202
3880:3060507
3838:7481781
3786:4408406
3737:5348765
3651:6110950
3519:3985467
3470:3515698
3418:1950709
3395:Bibcode
3363:9888800
3313:3380281
3292:Bibcode
3284:Science
3256:3271842
3167:2615623
3067:4572567
2930:4914116
2878:5215079
2827:3060507
2776:3089482
2648:2742777
2599:2464458
2551:9095198
2453:Bibcode
2445:Science
2421:2323259
2358:Bibcode
2335:8696976
2284:3985635
2173:2452083
2121:1707186
2101:Bibcode
2093:Science
2062:4132731
2017:8076225
1959:2746905
1819:E. coli
1809:E. coli
1797:E. coli
1793:E. coli
1776:E. coli
1746:History
1700:E. coli
1672:archaea
1535:viruses
1442:alanine
1375:RNASEH1
1348:RNase T
1333:calcium
1287:archaea
1141:PF01351
1099:during
1089:nucleus
1073:mammals
1055:E. coli
1048:during
961:PS50879
956:PROSITE
924:PF00075
913:RNase H
892:R-loops
845:E. coli
828:E. coli
769:β-sheet
682:E. coli
673:E. coli
657:archaea
641:E. coli
545:enzymes
524:of the
468:archaea
438:enzymes
423:RNase H
343:profile
326:MetaCyc
191:QuickGO
156:profile
139:MetaCyc
74:CAS no.
47:E. coli
18:RNase H
7252:Portal
7194:Lyases
6818:Drosha
6743:3.1.21
6711:RecBCD
6689:3.1.11
6309:PETase
6217:Lipase
5733:Primer
5363:(MeSH)
5334:
5327:373335
5324:
5285:
5250:
5240:
5191:
5181:
5150:
5140:
5091:
5050:
5009:
5002:356594
4999:
4960:
4942:Nature
4925:
4884:
4843:
4835:
4792:
4782:
4768:: 80.
4741:
4723:
4696:
4688:
4624:
4616:
4606:
4570:
4560:
4521:
4486:
4451:
4416:
4389:
4379:
4333:
4299:
4289:
4250:
4242:
4207:
4197:
4166:
4156:
4121:
4114:145536
4111:
4072:
4062:
4023:
4013:
3974:
3966:
3928:
3887:
3877:
3836:
3828:
3793:
3783:
3744:
3734:
3693:
3658:
3648:
3609:
3568:
3526:
3516:
3477:
3467:
3425:
3415:
3361:
3320:
3310:
3263:
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