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RNA polymerase

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1098: 1218:, PEP requires the presence of sigma (σ) factors for the recognition of its promoters, containing the -10 and -35 motifs. Despite the many commonalities between plant organellar and bacterial RNA polymerases and their structure, PEP additionally requires the association of a number of nuclear encoded proteins, termed PAPs (PEP-associated proteins), which form essential components that are closely associated with the PEP complex in plants. Initially, a group consisting of 10 PAPs was identified through biochemical methods, which was later extended to 12 PAPs. 551: 631:, a beta (β) subunit of 150 kDa, a beta prime subunit (β′) of 155 kDa, and a small omega (ω) subunit. A sigma (σ) factor binds to the core, forming the holoenzyme. After transcription starts, the factor can unbind and let the core enzyme proceed with its work. The core RNA polymerase complex forms a "crab claw" or "clamp-jaw" structure with an internal channel running along the full length. Eukaryotic and archaeal RNA polymerases have a similar core structure and work in a similar manner, although they have many extra subunits. 526: 915: 1002:, relies on a palindromic region of DNA. Transcribing the region causes the formation of a "hairpin" structure from the RNA transcription looping and binding upon itself. This hairpin structure is often rich in G-C base-pairs, making it more stable than the DNA-RNA hybrid itself. As a result, the 8 bp DNA-RNA hybrid in the transcription complex shifts to a 4 bp hybrid. These last 4 base pairs are weak A-U base pairs, and the entire RNA transcript will fall off the DNA. 655: 5514: 948:) residues in the RNAP will hold on to Mg ions, which will, in turn, coordinate the phosphates of the ribonucleotides. The first Mg will hold on to the α-phosphate of the NTP to be added. This allows the nucleophilic attack of the 3′-OH from the RNA transcript, adding another NTP to the chain. The second Mg will hold on to the pyrophosphate of the NTP. The overall reaction equation is: 251: 1299: 49: 815:. It is able to do this because specific interactions with the initiating nucleotide hold RNAP rigidly in place, facilitating chemical attack on the incoming nucleotide. Such specific interactions explain why RNAP prefers to start transcripts with ATP (followed by GTP, UTP, and then CTP). In contrast to 1057:
The β′ subunit is the largest subunit, and is encoded by the rpoC gene. The β′ subunit contains part of the active center responsible for RNA synthesis and contains some of the determinants for non-sequence-specific interactions with DNA and nascent RNA. It is split into two subunits in Cyanobacteria
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those of RNAP have only recently been investigated. Proofreading begins with separation of the mis-incorporated nucleotide from the DNA template. This pauses transcription. The polymerase then backtracks by one position and cleaves the dinucleotide that contains the mismatched nucleotide. In the RNA
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studies of both types of enzymes reveal that, other than containing a critical Mg ion at the catalytic site, they are virtually unrelated to each other; indeed template-dependent nucleotide polymerizing enzymes seem to have arisen independently twice during the early evolution of cells. One lineage
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more downstream DNA into the initiation complex. During the promoter escape transition, RNA polymerase is considered a "stressed intermediate." Thermodynamically the stress accumulates from the DNA-unwinding and DNA-compaction activities. Once the DNA-RNA heteroduplex is long enough (~10 bp), RNA
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have a single type of RNAP, responsible for the synthesis of all RNA. Archaeal RNAP is structurally and mechanistically similar to bacterial RNAP and eukaryotic nuclear RNAP I-V, and is especially closely structurally and mechanistically related to eukaryotic nuclear RNAP II. The history of the
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The 17-bp transcriptional complex has an 8-bp DNA-RNA hybrid, that is, 8 base-pairs involve the RNA transcript bound to the DNA template strand. As transcription progresses, ribonucleotides are added to the 3′ end of the RNA transcript and the RNAP complex moves along the DNA. The characteristic
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However, promoter escape is not the only outcome. RNA polymerase can also relieve the stress by releasing its downstream contacts, arresting transcription. The paused transcribing complex has two options: (1) release the nascent transcript and begin anew at the promoter or (2) reestablish a new
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RNA polymerase then starts to synthesize the initial DNA-RNA heteroduplex, with ribonucleotides base-paired to the template DNA strand according to Watson-Crick base-pairing interactions. As noted above, RNA polymerase makes contacts with the promoter region. However these stabilizing contacts
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Two copies of the α subunit, being the third-largest subunit, are present in a molecule of RNAP: α and α (one and two). Each α subunit contains two domains: αNTD (N-terminal domain) and αCTD (C-terminal domain). αNTD contains determinants for assembly of RNAP. αCTD (C-terminal domain) contains
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contain a multi-subunit RNAP ("PEP, plastid-encoded polymerase"). Due to its bacterial origin, the organization of PEP resembles that of current bacterial RNA polymerases: It is encoded by the RPOA, RPOB, RPOC1 and RPOC2 genes on the plastome, which as proteins form the core subunits of PEP,
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inhibit the enzyme's ability to access DNA further downstream and thus the synthesis of the full-length product. In order to continue RNA synthesis, RNA polymerase must escape the promoter. It must maintain promoter contacts while unwinding more downstream DNA for synthesis,
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synthesize RNA using a virally encoded multi-subunit RNAP. They are most similar to eukaryotic RNAPs, with some subunits minified or removed. Exactly which RNAP they are most similar to is a topic of debate. Most other viruses that synthesize RNA use unrelated mechanics.
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the beginning of sequence to be transcribed) and also, at some promoters, the α subunit C-terminal domain recognizing promoter upstream elements. There are multiple interchangeable sigma factors, each of which recognizes a distinct set of promoters. For example, in
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plays an important part in polymerase activity because of the unwinding and rewinding of DNA. Because regions of DNA in front of RNAP are unwound, there are compensatory positive supercoils. Regions behind RNAP are rewound and negative supercoils are present.
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Pfannschmidt T, Ogrzewalla K, Baginsky S, Sickmann A, Meyer HE, Link G (January 2000). "The multisubunit chloroplast RNA polymerase A from mustard (Sinapis alba L.). Integration of a prokaryotic core into a larger complex with organelle-specific functions".
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determinants for interaction with promoter DNA, making non-sequence-non-specific interactions at most promoters and sequence-specific interactions at upstream-element-containing promoters, and contains determinants for interactions with regulatory factors.
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SPβ uses YonO, a homolog of the β+β′ subunits of msRNAPs to form a monomeric (both barrels on the same chain) RNAP distinct from the usual "right hand" ssRNAP. It probably diverged very long ago from the canonical five-unit msRNAP, before the time of the
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to adapt to a changing environment, perform specialized roles within an organism, and maintain basic metabolic processes necessary for survival. Therefore, it is hardly surprising that the activity of RNAP is long, complex, and highly regulated. In
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complex, although TFS (TFIIS homolog) has been proposed as one based on similarity. There is an additional subunit dubbed Rpo13; together with Rpo5 it occupies a space filled by an insertion found in bacterial β′ subunits (1,377–1,420 in
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led to the modern DNA polymerases and reverse transcriptases, as well as to a few single-subunit RNA polymerases (ssRNAP) from phages and organelles. The other multi-subunit RNAP lineage formed all of the modern cellular RNA polymerases.
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Archaeal RNAP subunit previously used an "RpoX" nomenclature where each subunit is assigned a letter in a way unrelated to any other systems. In 2009, a new nomenclature based on Eukaryotic Pol II subunit "Rpb" numbering was proposed.
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After binding to the DNA, the RNA polymerase switches from a closed complex to an open complex. This change involves the separation of the DNA strands to form an unwound section of DNA of approximately 13 bp, referred to as the
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Transcription termination in eukaryotes is less well understood than in bacteria, but involves cleavage of the new transcript followed by template-independent addition of adenines at its new 3′ end, in a process called
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Schweer J, Türkeri H, Kolpack A, Link G (December 2010). "Role and regulation of plastid sigma factors and their functional interactors during chloroplast transcription - recent lessons from Arabidopsis thaliana".
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polymerase releases its upstream contacts and effectively achieves the promoter escape transition into the elongation phase. The heteroduplex at the active center stabilizes the elongation complex.
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gene. The β subunit contains the rest of the active center responsible for RNA synthesis and contains the rest of the determinants for non-sequence-specific interactions with DNA and nascent RNA.
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polymerase this occurs at the same active site used for polymerization and is therefore markedly different from the DNA polymerase where proofreading occurs at a distinct nuclease active site.
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Many viruses use a single-subunit DNA-dependent RNAP (ssRNAP) that is structurally and mechanistically related to the single-subunit RNAP of eukaryotic chloroplasts (RpoT) and mitochondria (
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Given that DNA and RNA polymerases both carry out template-dependent nucleotide polymerization, it might be expected that the two types of enzymes would be structurally related. However,
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have multiple types of nuclear RNAP, each responsible for synthesis of a distinct subset of RNA. All are structurally and mechanistically related to each other and to bacterial RNAP:
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before RNAP can initiate the DNA unwinding at that position. RNAP not only initiates RNA transcription, it also guides the nucleotides into position, facilitates attachment and
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Honda A, Mukaigawa J, Yokoiyama A, Kato A, Ueda S, Nagata K, et al. (April 1990). "Purification and molecular structure of RNA polymerase from influenza virus A/PR8".
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Hager DA, Jin DJ, Burgess RR (August 1990). "Use of Mono Q high-resolution ion-exchange chromatography to obtain highly pure and active Escherichia coli RNA polymerase".
4962: 214: 233: 1286:. RNAP I/III subunit AC40 found in some eukaryotes share similar sequences, but does not bind iron. This domain, in either case, serves a structural function. 452:
Bacteria and archaea only have one RNA polymerase. Eukaryotes have multiple types of nuclear RNAP, each responsible for synthesis of a distinct subset of RNA:
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discovery of the archaeal RNA polymerase is quite recent. The first analysis of the RNAP of an archaeon was performed in 1971, when the RNAP from the extreme
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RNA polymerase (purple) unwinding the DNA double helix. It uses one strand (darker orange) as a template to create the single-stranded messenger RNA (green).
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3′-OH on the nascent transcript at the active site via RNA polymerase's catalytic activity and recommence DNA scrunching to achieve promoter escape.
5134: 421:(multi-subunit RNAP) or only consist of one subunit (single-subunit RNAP, ssRNAP), each representing an independent lineage. The former is found in 1221:
Chloroplast also contain a second, structurally and mechanistically unrelated, single-subunit RNAP ("nucleus-encoded polymerase, NEP"). Eukaryotic
3163:"Nucleic acid enzymology of extremely halophilic bacteria. Halobacterium cutirubrum deoxyribonucleic acid-dependent ribonucleic acid polymerase" 1571:
Cermakian N, Ikeda TM, Miramontes P, Lang BF, Gray MW, Cedergren R (December 1997). "On the evolution of the single-subunit RNA polymerases".
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Chi W, He B, Mao J, Jiang J, Zhang L (September 2015). "Plastid sigma factors: Their individual functions and regulation in transcription".
3037:"Identification of essential subunits in the plastid-encoded RNA polymerase complex reveals building blocks for proper plastid development" 1644: 1678:
Griffiths AJF, Miller JH, Suzuki DT, et al. An Introduction to Genetic Analysis. 7th edition. New York: W. H. Freeman; 2000. Chapter 10.
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or "RNA genes"—a broad class of genes that encode RNA that is not translated into protein. The most prominent examples of RNA genes are
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gene). RNAP will preferentially release its RNA transcript at specific DNA sequences encoded at the end of genes, which are known as
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Roeder RG (November 1991). "The complexities of eukaryotic transcription initiation: regulation of preinitiation complex assembly".
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pictured during elongation. Portions of the enzyme were made transparent so as to make the path of RNA and DNA more clear. The
2508:(December 2000). "RNA polymerase: structural similarities between bacterial RNA polymerase and eukaryotic RNA polymerase II". 4117: 1357: 153: 5389: 177: 2411:
Lykke-Andersen S, Jensen TH (October 2007). "Overlapping pathways dictate termination of RNA polymerase II transcription".
863:"). In archaea and eukaryotes, the functions of the bacterial general transcription factor sigma are performed by multiple 5191: 5186: 4746: 4564: 4205: 4136: 3877: 5056: 4944: 4912: 4897: 3941: 1408: 1364: 864: 33: 4579: 2320: 1431: 5504: 4156: 1376: 1368: 550: 5374: 5490: 5477: 5464: 5451: 5438: 5425: 5412: 5177: 5155: 5130: 5105: 5025: 4633: 4593: 4538: 4515: 4487: 4455: 4321: 1265:
Archaea has the subunit corresponding to Eukaryotic Rpb1 split into two. There is no homolog to eukaryotic Rpb9 (
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The ω subunit is the smallest subunit. The ω subunit facilitates assembly of RNAP and stabilizes assembled RNAP.
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Werner F, Grohmann D (February 2011). "Evolution of multisubunit RNA polymerases in the three domains of life".
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In bacteria, termination of RNA transcription can be rho-dependent or rho-independent. The former relies on the
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RNA Polymerase II Transcription: the process of transcript elongation facilitated by disassembly of nucleosomes.
5534: 5338: 5281: 4642: 4623: 4554: 4288: 4200: 3988: 3901: 3870: 3821: 3815: 1246: 1229:(human), a nucleus-encoded single-subunit RNAP. Such phage-like polymerases are referred to as RpoT in plants. 1150:. This is the most studied type, and, due to the high level of control required over transcription, a range of 855:, σ is expressed under normal conditions and recognizes promoters for genes required under normal conditions (" 609: 171: 64: 1283: 1128:
45S (35S in yeast), which matures into 28S, 18S and 5.8S rRNAs, which will form the major RNA sections of the
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Fernández-Tornero C, Moreno-Morcillo M, Rashid UJ, Taylor NM, Ruiz FM, Gruene T, et al. (October 2013).
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Mathew R, Chatterji D (October 2006). "The evolving story of the omega subunit of bacterial RNA polymerase".
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for creating detailed molecular images of RNA polymerase during various stages of the transcription process.
5286: 4500: 4161: 3978: 3963: 1252: 832: 635: 306: 158: 1873:"A zinc-binding site in the largest subunit of DNA-dependent RNA polymerase is involved in enzyme assembly" 449:. Eukaryotic and archaeal RNAPs have more subunits than bacterial ones do, and are controlled differently. 4954: 4727: 4637: 4166: 4091: 3983: 2376:
Porrua O, Boudvillain M, Libri D (August 2016). "Transcription Termination: Variations on Common Themes".
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Monastyrskaya GS, Gubanov VV, Guryev SO, Salomatina IS, Shuvaeva TM, Lipkin VM, et al. (July 1982).
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T7 RNA polymerase producing a mRNA (green) from a DNA template. The protein is shown as a purple ribbon (
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structure did not find Rpo13 and only assigned the space to Rpo5/Rpb5. Rpo3 is notable in that it's an
146: 4249: 3433:"Diversification of giant and large eukaryotic dsDNA viruses predated the origin of modern eukaryotes" 3000:
Pfalz J, Pfannschmidt T (April 2013). "Essential nucleoid proteins in early chloroplast development".
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to the RNA strand is known as elongation; in eukaryotes, RNAP can build chains as long as 2.4 million
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Richardson JP (September 2002). "Rho-dependent termination and ATPases in transcript termination".
1258: 914: 903: 659: 76: 174: 5276: 4848: 4786: 4737: 4472: 4299: 4149: 4032: 3621: 3307: 2862: 2602:"Evolutionary relationships among eubacteria, cyanobacteria, and chloroplasts: Evidence from the 2505: 2145:"Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS" 2083: 1614: 1518: 1445: 1157: 1106: 860: 707: 481: 98: 2274:
Sydow JF, Cramer P (December 2009). "RNA polymerase fidelity and transcriptional proofreading".
1438: 998:, which destabilizes the DNA-RNA heteroduplex and causes RNA release. The latter, also known as 1787:
Korkhin Y, Unligil UM, Littlefield O, Nelson PJ, Stuart DI, Sigler PB, et al. (May 2009).
1375:, both of which exist for a portion of their life cycle as double-stranded RNA. However, some 666:
decorated by hundreds of RNAP molecules too small to be resolved. Each RNAP is transcribing an
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that work together. The RNA polymerase-promoter closed complex is usually referred to as the "
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In order to bind promoters, RNAP core associates with the transcription initiation factor
1007: 687: 418: 322: 134: 3601: 3507: 3492:"Single-peptide DNA-dependent RNA polymerase homologous to multi-subunit RNA polymerase" 3448: 3342: 3287: 3230: 2840: 2463: 2103: 2042: 2027:"Abortive initiation and productive initiation by RNA polymerase involve DNA scrunching" 1584: 110: 5518: 5407: 5348: 5087: 4926: 4702: 4665: 4037: 3524: 3491: 3467: 3432: 3408: 3383: 3359: 3326: 3247: 3214: 3187: 3162: 3061: 3036: 2906: 2881: 2800: 2783: 2251: 2226: 2120: 2087: 2059: 2026: 1815: 1788: 1461: 1424: 1396: 1332: 1102: 1040: 973: 894: 816: 751: 691: 654: 446: 209: 69: 3709: 3692: 3549:"The Extended "Two-Barrel" Polymerases Superfamily: Structure, Function and Evolution" 2759: 2734: 2701: 2634: 2601: 2577: 2544: 2354: 1897: 1872: 1789:"Evolution of complex RNA polymerases: the complete archaeal RNA polymerase structure" 1755: 1738: 1714: 1689: 1542: 189: 5528: 5312: 5271: 4356: 4238: 3925: 3311: 3138: 3121: 2943: 2866: 2625: 2482: 2447: 1985: 1737:
Zhang G, Campbell EA, Minakhin L, Richter C, Severinov K, Darst SA (September 1999).
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Ahlquist P (May 2002). "RNA-dependent RNA polymerases, viruses, and RNA silencing".
1522: 510:. In addition to the ssRNAPs, chloroplasts also encode and use a bacteria-like RNAP. 5539: 5261: 4445: 4415: 4344: 4112: 4042: 3911: 1933: 1618: 1404: 1222: 1173: 1086: 880: 843: 769: 755: 489: 442: 352: 3013: 846:
recognizing the core promoter region containing the −35 and −10 elements (located
3858: 3843: 2978: 2424: 2242: 2161: 2144: 1959: 1805: 5485: 5420: 5256: 5011: 5001: 4602: 4339: 4280: 4215: 4144: 1739:"Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution" 1407:
for the discovery of what was believed to be RNAP, but instead turned out to be
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Proceedings of the National Academy of Sciences of the United States of America
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Proceedings of the National Academy of Sciences of the United States of America
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Ishihama A (2000). "Functional modulation of Escherichia coli RNA polymerase".
1705: 675: 671: 301:, RNAP locally opens the double-stranded DNA so that one strand of the exposed 4813: 4656: 4569: 4334: 4284: 4173: 3565: 3548: 2670: 2448:"Amitochondriate amoebae and the evolution of DNA-dependent RNA polymerase II" 2389: 2287: 1657: 995: 773: 723: 715: 628: 620: 433:
alike, sharing a similar core structure and mechanism. The latter is found in
359: 345: 302: 2750: 2568: 2472: 1857: 348:(so-called "RNA genes"). Examples of four functional types of RNA genes are: 5459: 5433: 5092: 5005: 4542: 4308: 3609: 3457: 2849: 2824: 2196:"Cell Biology by the Numbers: What is faster, transcription or translation?" 2111: 2050: 1242: 1169: 1113: 933: 922: 792: 643: 485: 475: 430: 386: 330: 250: 3808:– DNA Interactive, including information and Flash clips on RNA Polymerase. 3666: 3657: 3640: 3617: 3574: 3533: 3476: 3417: 3368: 3303: 3256: 3147: 3106: 3070: 3021: 2986: 2951: 2915: 2858: 2768: 2678: 2529: 2521: 2432: 2397: 2362: 2305: 2260: 2180: 2129: 2068: 1941: 1906: 1888: 1842:(Sixth ed.). New York, NY: Garland Science, Taylor and Francis Group. 1824: 1764: 1723: 1550: 1514: 859:"), while σ recognizes promoters for genes required at high temperatures (" 3844:
3D macromolecular structures of RNA Polymerase from the EM Data Bank(EMDB)
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Lee Y, Kim M, Han J, Yeom KH, Lee S, Baek SH, et al. (October 2004).
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elongation rates in prokaryotes and eukaryotes are about 10–100 nts/sec.
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Guglielmini J, Woo AC, Krupovic M, Forterre P, Gaia M (September 2019).
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Regulation of mammalian ribosomal gene transcription by RNA polymerase I
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Structure of eukaryotic RNA polymerase II (light blue) in complex with
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respectively named α, β, β′ and β″. Similar to the RNA polymerase in
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can be used as a template for the synthesis of RNA, a process called
283: 221: 117: 105: 93: 2784:"RNA polymerase III. Genes, factors and transcriptional specificity" 674:
of the DNA, where RNAP initiates transcription; "End" indicates the
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Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression
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Watson JD, Baker TA, Bell SP, Gann AA, Levine M, Losick RM (2013).
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The β subunit is the second-largest subunit, and is encoded by the
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RNAP can initiate transcription at specific DNA sequences known as
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set the total number of identified archaeal subunits at thirteen.
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RNAP is a large molecule. The core enzyme has five subunits (~400
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CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase
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Markov D, Naryshkina T, Mustaev A, Severinov K (September 1999).
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Finn RD, Orlova EV, Gowen B, Buck M, van Heel M (December 2000).
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Steiner S, Schröter Y, Pfalz J, Pfannschmidt T (November 2011).
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Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms
1690:"Escherichia coli RNA polymerase core and holoenzyme structures" 1165: 1161: 1139: 1125: 1065: 1036: 823:
activity, therefore no separate enzyme is needed to unwind DNA.
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RNA polymerase is essential to life, and is found in all living
129: 5215: 4253: 3866: 2882:"RNA polymerase V transcription guides ARGONAUTE4 to chromatin" 48: 3921: 3325:
Jennings ME, Lessner FH, Karr EA, Lessner DJ (February 2017).
1339:. Perhaps the most widely studied such single-subunit RNAP is 667: 663: 291: 287: 627:
consists of five subunits: two alpha (α) subunits of 36 
3215:"The X-ray crystal structure of RNA polymerase from Archaea" 1250:
was isolated and purified. Crystal structures of RNAPs from
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RNAP produces RNA that, functionally, is either for protein
333:, RNAP can build chains as long as 2.4 million nucleotides. 5211: 2321:"What is the error rate in transcription and translation?" 2025:
Revyakin A, Liu C, Ebright RH, Strick TR (November 2006).
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Cramer P (February 2002). "Multisubunit RNA polymerases".
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Herr AJ, Jensen MB, Dalmay T, Baulcombe DC (April 2005).
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chains at the ribosomal site of protein synthesis during
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have been identified, which modify the activity of RNAP.
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Wierzbicki AT, Ream TS, Haag JR, Pikaard CS (May 2009).
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Forrest D, James K, Yuzenkova Y, Zenkin N (June 2017).
2825:"RNA polymerase IV directs silencing of endogenous DNA" 2227:"Basic mechanism of transcription by RNA polymerase II" 417:. Depending on the organism, a RNA polymerase can be a 3849:
This article incorporates text from the public domain
3805: 3272:"Crystal structure of the 14-subunit RNA polymerase I" 2143:
Kettenberger H, Armache KJ, Cramer P (December 2004).
2088:"Direct detection of abortive RNA transcripts in vivo" 1419:
RNA polymerase can be isolated in the following ways:
286:
that catalyzes the chemical reactions that synthesize
5502: 5052:
CDP-diacylglycerol—inositol 3-phosphatidyltransferase
2735:"MicroRNA genes are transcribed by RNA polymerase II" 1645:"Structural biology: How proteins got their close-up" 762:(rRNA), both of which are involved in the process of 5057:
CDP-diacylglycerol—choline O-phosphatidyltransferase
3122:"Structure and function of archaeal RNA polymerases" 5398: 5362: 5331: 5300: 5249: 5176: 5154: 5129: 5104: 5085: 5065: 5047:
CDP-diacylglycerol—serine O-phosphatidyltransferase
5034: 5024: 4994: 4976: 4953: 4925: 4824: 4664: 4655: 4632: 4592: 4537: 4514: 4486: 4320: 4296: 4226: 4135: 4100: 4074: 4065: 4023: 3997: 3971: 3962: 3900: 2446:Stiller JW, Duffield EC, Hall BD (September 1998). 1391:RNAP was discovered independently by Charles Loe, 232: 220: 208: 203: 183: 164: 152: 140: 128: 116: 104: 92: 87: 75: 63: 58: 41: 2553:gene and amino acid sequence of the beta′-subunit" 936:ion (yellow) is located at the enzyme active site. 714:to the template DNA strand. The process of adding 405:Functions as an enzymatically active RNA molecule. 3213:Hirata A, Klein BJ, Murakami KS (February 2008). 3830:RNA Polymerase – Synthesis RNA from DNA Template 842:RNA polymerase binding in bacteria involves the 646:cations which aid in the transcription process. 3208: 3206: 1452:And also combinations of the above techniques. 506:found in plants are less understood; they make 1782: 1780: 1778: 1776: 1774: 1488: 1486: 1484: 1482: 5227: 4265: 3878: 3382:Mirzakhanyan Y, Gershon PD (September 2017). 1566: 1564: 1562: 1560: 1399:in 1960. By this time, one half of the 1959 1035:, the same enzyme catalyzes the synthesis of 8: 5073:N-acetylglucosamine-1-phosphate transferase 4963:UTP—glucose-1-phosphate uridylyltransferase 2549:RNA polymerase, Nucleotide sequence of the 980:The overall error rate is around 10 to 10. 392:Regulates gene activity; and, RNA silencing 5234: 5220: 5212: 5101: 5031: 4661: 4652: 4317: 4272: 4258: 4250: 4071: 4033:Precursor mRNA (pre-mRNA / hnRNA) 3968: 3885: 3871: 3863: 3388:Microbiology and Molecular Biology Reviews 1154:are required for its binding to promoters. 833:Transcription (biology) § Major steps 710:. It then produces an RNA chain, which is 572:Homologous subunits are colored the same: 200: 5167:serine/threonine-specific protein kinases 5145:serine/threonine-specific protein kinases 4968:Galactose-1-phosphate uridylyltransferase 3814:at the U.S. National Library of Medicine 3708: 3656: 3564: 3523: 3466: 3456: 3407: 3358: 3246: 3186: 3137: 3060: 2905: 2848: 2799: 2758: 2633: 2576: 2481: 2471: 2295: 2250: 2170: 2160: 2119: 2058: 1896: 1814: 1804: 1754: 1713: 1656: 1592: 1278:). An earlier, lower-resolution study on 474:synthesizes precursors of mRNAs and most 5509: 2600:Bergsland KJ, Haselkorn R (June 1991). 2005: 2003: 1478: 972:Unlike the proofreading mechanisms of 38: 4053:Histone acetylation and deacetylation 3746:10.1093/oxfordjournals.jbchem.a123097 2276:Current Opinion in Structural Biology 1531:Current Opinion in Structural Biology 484:synthesizes tRNAs, rRNA 5S and other 276:DNA-directed/dependent RNA polymerase 7: 4118:Ribosome-nascent chain complex (RNC) 2225:Svetlov V, Nudler E (January 2013). 802:)—enzymatically active RNA molecules 27:Enzyme that synthesizes RNA from DNA 3697:The Journal of Biological Chemistry 3691:Kelly JL, Lehman IR (August 1986). 3645:The Journal of Biological Chemistry 3161:Louis BG, Fitt PS (February 1971). 1383:, also contain RNA-dependent RNAP. 1321:nucleocytoplasmic large DNA viruses 869:transcription preinitiation complex 2801:10.1111/j.1432-1033.1993.tb17626.x 2206:from the original on 20 April 2017 686:transcription affects patterns of 25: 4478:Glucose-1,6-bisphosphate synthase 3641:"The discovery of RNA polymerase" 313:and its associated transcription 53:RNA polymerase hetero27mer, human 5512: 4619:Ribose-phosphate diphosphokinase 3139:10.1111/j.1365-2958.2007.05876.x 3087:European Journal of Cell Biology 2944:10.1046/j.1432-1327.2000.00991.x 2932:European Journal of Biochemistry 2788:European Journal of Biochemistry 2626:10.1128/jb.173.11.3446-3455.1991 1432:glycerol gradient centrifugation 1403:in Medicine had been awarded to 1105:(red), a strong poison found in 549: 524: 366:chains at the ribosomal site of 47: 4123:Post-translational modification 789:(rRNA)—a component of ribosomes 2969:. SI: Chloroplast Biogenesis. 2297:11858/00-001M-0000-0015-837E-8 2172:11858/00-001M-0000-0015-84E1-D 1974:Trends in Biochemical Sciences 1934:10.1146/annurev.micro.54.1.499 1573:Journal of Molecular Evolution 1358:last universal common ancestor 1109:that targets this vital enzyme 556:Yeast RNA polymerase II core ( 1: 5192:Protein-histidine tele-kinase 5187:Protein-histidine pros-kinase 5066:Glycosyl-1-phosphotransferase 3710:10.1016/S0021-9258(18)67529-5 3014:10.1016/j.tplants.2012.11.003 2967:Biochimica et Biophysica Acta 2702:10.1016/S0079-6603(08)60506-1 2355:10.1016/S0167-4781(02)00456-6 2012:Molecular Biology of the Gene 1922:Annual Review of Microbiology 1840:Molecular Biology of the Cell 1756:10.1016/S0092-8674(00)81515-9 1632:Nobel Prize in Chemistry 2006 1543:10.1016/s0959-440x(02)00294-4 1196:synthesizes RNAs involved in 865:general transcription factors 4898:RNA-dependent RNA polymerase 3553:Journal of Molecular Biology 3547:Sauguet L (September 2019). 2979:10.1016/j.bbabio.2015.01.001 2510:Journal of Molecular Biology 2425:10.1016/j.biochi.2007.05.007 2243:10.1016/j.bbagrm.2012.08.009 2162:10.1016/j.molcel.2004.11.040 1986:10.1016/0968-0004(91)90164-Q 1806:10.1371/journal.pbio.1000102 1495:Nature Reviews. Microbiology 1409:polynucleotide phosphorylase 1346:. ssRNAPs cannot proofread. 383:Incorporates into ribosomes; 34:RNA-dependent RNA polymerase 18:DNA-dependent RNA polymerase 4805:RNA-directed DNA polymerase 4673:DNA-directed DNA polymerase 3639:Hurwitz J (December 2005). 3120:Werner F (September 2007). 2782:Willis IM (February 1993). 1643:Stoddart C (1 March 2022). 1377:positive strand RNA viruses 1369:negative strand RNA viruses 445:, and is related to modern 42:DNA-directed RNA polymerase 5566: 5158:: protein-dual-specificity 3848: 3099:10.1016/j.ejcb.2010.06.016 2545:"The primary structure of 1331:) and, more distantly, to 1138:synthesizes precursors of 987: 830: 772:(tRNA)—transfers specific 733:Products of RNAP include: 682:Control of the process of 31: 5390:Michaelis–Menten kinetics 3566:10.1016/j.jmb.2019.05.017 2671:10.1016/j.tim.2006.08.002 2390:10.1016/j.tig.2016.05.007 2288:10.1016/j.sbi.2009.10.009 2086:, Nickels BE (May 2009). 1658:10.1146/knowable-022822-1 460:synthesizes a pre-rRNA 45 199: 46: 5282:Diffusion-limited enzyme 5135:protein-serine/threonine 5035:Phosphatidyltransferases 4624:Thiamine diphosphokinase 4184:sequestration (P-bodies) 3816:Medical Subject Headings 2751:10.1038/sj.emboj.7600385 2473:10.1073/pnas.95.20.11769 2014:(7th ed.). Pearson. 1838:Alberts B (2014-11-18). 1706:10.1093/emboj/19.24.6833 1247:Halobacterium cutirubrum 795:—regulates gene activity 740:(mRNA)—template for the 722:(the full length of the 699:bacteria, more than 100 634:All RNAPs contain metal 610:Nobel Prize in Chemistry 274:), or more specifically 4162:Gene regulatory network 3734:Journal of Biochemistry 3610:10.1126/science.1069132 3458:10.1073/pnas.1912006116 3167:The Biochemical Journal 3002:Trends in Plant Science 2850:10.1126/science.1106910 2614:Journal of Bacteriology 2112:10.1126/science.1169237 2051:10.1126/science.1131398 1877:Genes & Development 1425:phosphocellulose column 1253:Sulfolobus solfataricus 690:and, thereby, allows a 583: yellow: α2/RPB11, 4955:Nucleotidyltransferase 4638:nucleotidyltransferase 4565:Nucleoside-diphosphate 4167:cis-regulatory element 3658:10.1074/jbc.X500006200 3126:Molecular Microbiology 2659:Trends in Microbiology 2569:10.1093/nar/10.13.4035 2557:Nucleic Acids Research 2522:10.1006/jmbi.2000.4309 1889:10.1101/gad.13.18.2439 1527:See also Cramer 2002: 1337:reverse transcriptases 1313: 1110: 1041:non-coding RNA (ncRNA) 1020:x-ray crystallographic 937: 919: 679: 577: orange: α1/RPB3, 437:as well as eukaryotic 317:must be attached to a 255: 5375:Eadie–Hofstee diagram 5308:Allosteric regulation 4809:Reverse transcriptase 3496:Nature Communications 3400:10.1128/MMBR.00010-17 3053:10.1104/pp.111.184515 1363:Other viruses use an 1301: 1152:transcription factors 1100: 1000:intrinsic termination 990:Terminator (genetics) 925: 917: 742:synthesis of proteins 701:transcription factors 657: 534:RNA polymerase core ( 253: 5385:Lineweaver–Burk plot 4598:diphosphotransferase 4580:Thiamine-diphosphate 4287:-containing groups ( 4189:alternative splicing 4179:Post-transcriptional 4005:Transcription factor 2610:sp. strain PCC 7120" 1204:formation in plants. 877:transcription bubble 589: wheat: β/RPB2, 311:transcription factor 5180:: protein-histidine 5098:; protein acceptor) 4986:mRNA capping enzyme 4978:Guanylyltransferase 4113:Transfer RNA (tRNA) 3781:10.1021/bi00486a016 3703:(22): 10340–10347. 3651:(52): 42477–42485. 3602:2002Sci...296.1270A 3596:(5571): 1270–1273. 3516:10.1038/ncomms15774 3508:2017NatCo...815774F 3449:2019PNAS..11619585G 3443:(39): 19585–19592. 3343:2017MBioO...6..399J 3296:10.1038/nature12636 3288:2013Natur.502..644F 3239:10.1038/nature06530 3231:2008Natur.451..851H 2841:2005Sci...308..118H 2464:1998PNAS...9511769S 2458:(20): 11769–11774. 2319:Philips R, Milo R. 2200:book.bionumbers.org 2194:Milo R, Philips R. 2104:2009Sci...324..927G 2043:2006Sci...314.1139R 2037:(5802): 1139–1143. 1585:1997JMolE..45..671C 1507:10.1038/nrmicro2507 1284:iron–sulfur protein 1259:Sulfolobus shibatae 1107:death cap mushrooms 904:Abortive initiation 660:electron-micrograph 601: pink: ω/RPB6. 595: red: β′/RPB1, 358:Transfers specific 5344:Enzyme superfamily 5277:Enzyme promiscuity 4456:Phosphoinositide 3 4300:phosphotransferase 4227:Influential people 4206:Post-translational 4025:Post-transcription 2378:Trends in Genetics 1603:10.1007/PL00006271 1446:ion chromatography 1365:RNA-dependent RNAP 1314: 1158:RNA polymerase III 1124:synthesizes a pre- 1111: 938: 920: 857:housekeeping genes 808:RNAP accomplishes 680: 482:RNA polymerase III 256: 5500: 5499: 5209: 5208: 5205: 5204: 5081: 5080: 5020: 5019: 4921: 4920: 4834:Template-directed 4588: 4587: 4555:Phosphomevalonate 4247: 4246: 4131: 4130: 4061: 4060: 3937:Special transfers 3775:(34): 7890–7894. 3559:(20): 4167–4183. 3282:(7473): 644–649. 3225:(7180): 851–854. 3179:10.1042/bj1210621 2835:(5718): 118–120. 2745:(20): 4051–4060. 2692:Grummt I (1999). 2620:(11): 3446–3455. 2563:(13): 4035–4044. 2419:(10): 1177–1182. 2098:(5929): 927–928. 1883:(18): 2439–2448. 1700:(24): 6833–6844. 1649:Knowable Magazine 1344:T7 RNA polymerase 1184:RNA polymerase IV 1136:RNA polymerase II 1058:and chloroplasts. 614:Roger D. Kornberg 500:RNA polymerase IV 472:RNA polymerase II 368:protein synthesis 297:Using the enzyme 260:molecular biology 248: 247: 244: 243: 147:metabolic pathway 16:(Redirected from 5557: 5517: 5516: 5508: 5380:Hanes–Woolf plot 5323:Enzyme activator 5318:Enzyme inhibitor 5292:Enzyme catalysis 5236: 5229: 5222: 5213: 5197:Histidine kinase 5120:tyrosine kinases 5110:protein-tyrosine 5102: 5032: 4839:RNA polymerase I 4662: 4653: 4506:Aspartate kinase 4501:Phosphoglycerate 4318: 4274: 4267: 4260: 4251: 4072: 3969: 3887: 3880: 3873: 3864: 3793: 3792: 3764: 3758: 3757: 3729: 3723: 3722: 3712: 3688: 3682: 3680:Nobel Prize 1959 3677: 3671: 3670: 3660: 3636: 3630: 3629: 3585: 3579: 3578: 3568: 3544: 3538: 3537: 3527: 3487: 3481: 3480: 3470: 3460: 3428: 3422: 3421: 3411: 3379: 3373: 3372: 3362: 3351:10.1002/mbo3.399 3331:MicrobiologyOpen 3322: 3316: 3315: 3267: 3261: 3260: 3250: 3210: 3201: 3200: 3190: 3158: 3152: 3151: 3141: 3132:(6): 1395–1404. 3117: 3111: 3110: 3081: 3075: 3074: 3064: 3047:(3): 1043–1055. 3041:Plant Physiology 3032: 3026: 3025: 2997: 2991: 2990: 2962: 2956: 2955: 2926: 2920: 2919: 2909: 2877: 2871: 2870: 2852: 2820: 2814: 2813: 2803: 2779: 2773: 2772: 2762: 2739:The EMBO Journal 2730: 2724: 2723: 2689: 2683: 2682: 2654: 2648: 2647: 2637: 2597: 2591: 2590: 2580: 2540: 2534: 2533: 2502: 2496: 2495: 2485: 2475: 2443: 2437: 2436: 2408: 2402: 2401: 2373: 2367: 2366: 2338: 2332: 2331: 2329: 2327: 2316: 2310: 2309: 2299: 2271: 2265: 2264: 2254: 2222: 2216: 2215: 2213: 2211: 2191: 2185: 2184: 2174: 2164: 2140: 2134: 2133: 2123: 2079: 2073: 2072: 2062: 2022: 2016: 2015: 2007: 1998: 1997: 1969: 1963: 1952: 1946: 1945: 1917: 1911: 1910: 1900: 1868: 1862: 1861: 1835: 1829: 1828: 1818: 1808: 1784: 1769: 1768: 1758: 1734: 1728: 1727: 1717: 1694:The EMBO Journal 1685: 1679: 1676: 1670: 1669: 1667: 1665: 1660: 1640: 1634: 1629: 1623: 1622: 1596: 1568: 1555: 1554: 1526: 1490: 1311: 1194:RNA polymerase V 1122:RNA polymerase I 861:heat-shock genes 819:, RNAP includes 697:Escherichia coli 638:, in particular 600: 594: 588: 582: 576: 565: 553: 543: 528: 458:RNA polymerase I 319:DNA binding site 315:mediator complex 201: 51: 39: 21: 5565: 5564: 5560: 5559: 5558: 5556: 5555: 5554: 5535:Gene expression 5525: 5524: 5523: 5511: 5503: 5501: 5496: 5408:Oxidoreductases 5394: 5370:Enzyme kinetics 5358: 5354:List of enzymes 5327: 5296: 5267:Catalytic triad 5245: 5240: 5210: 5201: 5172: 5150: 5125: 5096: 5090: 5086:2.7.10-2.7.13: 5077: 5061: 5028:: miscellaneous 5016: 4990: 4972: 4949: 4932:exoribonuclease 4929: 4917: 4903:Polyadenylation 4820: 4646: 4640: 4628: 4610: 4606: 4600: 4584: 4546: 4533: 4510: 4482: 4312: 4306: 4298: 4292: 4278: 4248: 4243: 4222: 4157:Transcriptional 4127: 4096: 4057: 4048:Polyadenylation 4019: 3993: 3958: 3952:Protein→Protein 3903: 3896: 3894:Gene expression 3891: 3861: 3837:Wayback Machine 3802: 3797: 3796: 3766: 3765: 3761: 3731: 3730: 3726: 3690: 3689: 3685: 3678: 3674: 3638: 3637: 3633: 3587: 3586: 3582: 3546: 3545: 3541: 3489: 3488: 3484: 3430: 3429: 3425: 3381: 3380: 3376: 3324: 3323: 3319: 3269: 3268: 3264: 3212: 3211: 3204: 3160: 3159: 3155: 3119: 3118: 3114: 3093:(12): 940–946. 3083: 3082: 3078: 3034: 3033: 3029: 2999: 2998: 2994: 2964: 2963: 2959: 2928: 2927: 2923: 2886:Nature Genetics 2879: 2878: 2874: 2822: 2821: 2817: 2781: 2780: 2776: 2732: 2731: 2727: 2712: 2691: 2690: 2686: 2665:(10): 450–455. 2656: 2655: 2651: 2599: 2598: 2594: 2542: 2541: 2537: 2504: 2503: 2499: 2445: 2444: 2440: 2410: 2409: 2405: 2375: 2374: 2370: 2340: 2339: 2335: 2325: 2323: 2318: 2317: 2313: 2273: 2272: 2268: 2224: 2223: 2219: 2209: 2207: 2193: 2192: 2188: 2142: 2141: 2137: 2081: 2080: 2076: 2024: 2023: 2019: 2009: 2008: 2001: 1980:(11): 402–408. 1971: 1970: 1966: 1953: 1949: 1919: 1918: 1914: 1870: 1869: 1865: 1850: 1837: 1836: 1832: 1799:(5): e1000102. 1786: 1785: 1772: 1736: 1735: 1731: 1687: 1686: 1682: 1677: 1673: 1663: 1661: 1642: 1641: 1637: 1630: 1626: 1594:10.1.1.520.3555 1570: 1569: 1558: 1528: 1492: 1491: 1480: 1475: 1458: 1417: 1389: 1333:DNA polymerases 1319:and some other 1317:Orthopoxviruses 1303: 1296: 1280:S. solfataricus 1235: 1207: 1202:heterochromatin 1095: 1029: 1016: 1014:Other organisms 1008:polyadenylation 992: 986: 970: 963: 959: 955: 912: 890: 888:Promoter escape 840: 835: 829: 798:Catalytic RNA ( 688:gene expression 652: 612:was awarded to 606: 605: 604: 603: 602: 598: 596: 592: 590: 586: 584: 580: 578: 574: 569: 568: 567: 557: 554: 546: 545: 535: 529: 518: 513: 447:DNA polymerases 419:protein complex 323:promoter region 54: 37: 28: 23: 22: 15: 12: 11: 5: 5563: 5561: 5553: 5552: 5547: 5542: 5537: 5527: 5526: 5522: 5521: 5498: 5497: 5495: 5494: 5481: 5468: 5455: 5442: 5429: 5416: 5402: 5400: 5396: 5395: 5393: 5392: 5387: 5382: 5377: 5372: 5366: 5364: 5360: 5359: 5357: 5356: 5351: 5346: 5341: 5335: 5333: 5332:Classification 5329: 5328: 5326: 5325: 5320: 5315: 5310: 5304: 5302: 5298: 5297: 5295: 5294: 5289: 5284: 5279: 5274: 5269: 5264: 5259: 5253: 5251: 5247: 5246: 5241: 5239: 5238: 5231: 5224: 5216: 5207: 5206: 5203: 5202: 5200: 5199: 5194: 5189: 5183: 5181: 5174: 5173: 5171: 5170: 5161: 5159: 5152: 5151: 5149: 5148: 5139: 5137: 5127: 5126: 5124: 5123: 5114: 5112: 5099: 5094: 5088:protein kinase 5083: 5082: 5079: 5078: 5076: 5075: 5069: 5067: 5063: 5062: 5060: 5059: 5054: 5049: 5044: 5038: 5036: 5029: 5022: 5021: 5018: 5017: 5015: 5014: 5009: 4998: 4996: 4992: 4991: 4989: 4988: 4982: 4980: 4974: 4973: 4971: 4970: 4965: 4959: 4957: 4951: 4950: 4948: 4947: 4942: 4936: 4934: 4927:Phosphorolytic 4923: 4922: 4919: 4918: 4916: 4915: 4910: 4905: 4900: 4895: 4894: 4893: 4888: 4883: 4873: 4872: 4871: 4861: 4856: 4851: 4846: 4841: 4836: 4830: 4828: 4826:RNA polymerase 4822: 4821: 4819: 4818: 4817: 4816: 4806: 4802: 4801: 4800: 4799: 4794: 4789: 4778: 4777: 4776: 4771: 4766: 4761: 4750: 4744: 4743: 4742: 4735: 4730: 4725: 4720: 4709: 4708: 4707: 4700: 4695: 4690: 4685: 4674: 4670: 4668: 4666:DNA polymerase 4659: 4650: 4644: 4630: 4629: 4627: 4626: 4621: 4615: 4613: 4608: 4604: 4590: 4589: 4586: 4585: 4583: 4582: 4577: 4572: 4567: 4562: 4557: 4551: 4549: 4544: 4535: 4534: 4532: 4531: 4525: 4523: 4512: 4511: 4509: 4508: 4503: 4497: 4495: 4484: 4483: 4481: 4480: 4475: 4470: 4469: 4468: 4463: 4453: 4451:Diacylglycerol 4448: 4443: 4438: 4433: 4428: 4423: 4418: 4413: 4412: 4411: 4401: 4396: 4391: 4390: 4389: 4384: 4379: 4374: 4369: 4362:Phosphofructo- 4359: 4354: 4353: 4352: 4342: 4337: 4331: 4329: 4315: 4310: 4294: 4293: 4279: 4277: 4276: 4269: 4262: 4254: 4245: 4244: 4242: 4241: 4236: 4234:François Jacob 4230: 4228: 4224: 4223: 4221: 4220: 4219: 4218: 4213: 4203: 4198: 4197: 4196: 4191: 4186: 4176: 4171: 4170: 4169: 4164: 4154: 4153: 4152: 4141: 4139: 4133: 4132: 4129: 4128: 4126: 4125: 4120: 4115: 4110: 4104: 4102: 4098: 4097: 4095: 4094: 4089: 4084: 4078: 4076: 4069: 4063: 4062: 4059: 4058: 4056: 4055: 4050: 4045: 4040: 4035: 4029: 4027: 4021: 4020: 4018: 4017: 4012: 4010:RNA polymerase 4007: 4001: 3999: 3995: 3994: 3992: 3991: 3986: 3981: 3975: 3973: 3966: 3960: 3959: 3957: 3956: 3955: 3954: 3949: 3944: 3934: 3933: 3932: 3914: 3908: 3906: 3898: 3897: 3892: 3890: 3889: 3882: 3875: 3867: 3847: 3846: 3833: 3832: 3827: 3819: 3812:RNA+Polymerase 3809: 3801: 3800:External links 3798: 3795: 3794: 3759: 3740:(4): 624–628. 3724: 3683: 3672: 3631: 3580: 3539: 3482: 3423: 3374: 3317: 3262: 3202: 3173:(4): 621–627. 3153: 3112: 3076: 3027: 2992: 2973:(9): 770–778. 2957: 2938:(1): 253–261. 2921: 2898:10.1038/ng.365 2892:(5): 630–634. 2872: 2815: 2774: 2725: 2710: 2684: 2649: 2592: 2535: 2516:(5): 687–698. 2497: 2438: 2403: 2384:(8): 508–522. 2368: 2349:(2): 251–260. 2333: 2311: 2282:(6): 732–739. 2266: 2217: 2186: 2155:(6): 955–965. 2149:Molecular Cell 2135: 2074: 2017: 1999: 1964: 1947: 1912: 1863: 1848: 1830: 1770: 1749:(6): 811–824. 1729: 1680: 1671: 1635: 1624: 1579:(6): 671–681. 1556: 1477: 1476: 1474: 1471: 1470: 1469: 1464: 1462:Alpha-amanitin 1457: 1454: 1450: 1449: 1442: 1435: 1428: 1416: 1413: 1397:Jerard Hurwitz 1393:Audrey Stevens 1388: 1385: 1295: 1292: 1234: 1231: 1206: 1205: 1191: 1181: 1155: 1133: 1118: 1094: 1091: 1083: 1082: 1079: 1076: 1072: 1069: 1062: 1059: 1055: 1028: 1025: 1015: 1012: 988:Main article: 985: 982: 974:DNA polymerase 969: 966: 965: 964: 961: 957: 953: 911: 908: 889: 886: 839: 836: 828: 825: 817:DNA polymerase 806: 805: 804: 803: 796: 790: 784: 752:Non-coding RNA 749: 651: 648: 597: 591: 585: 579: 573: 571: 570: 555: 548: 547: 530: 523: 522: 521: 520: 519: 517: 514: 512: 511: 497: 479: 478:and microRNAs. 469: 454: 407: 406: 403: 393: 390: 384: 381: 375: 356: 266:(abbreviated 264:RNA polymerase 246: 245: 242: 241: 236: 230: 229: 224: 218: 217: 212: 206: 205: 197: 196: 187: 181: 180: 169: 162: 161: 156: 150: 149: 144: 138: 137: 132: 126: 125: 120: 114: 113: 108: 102: 101: 96: 90: 89: 85: 84: 79: 73: 72: 67: 61: 60: 56: 55: 52: 44: 43: 26: 24: 14: 13: 10: 9: 6: 4: 3: 2: 5562: 5551: 5548: 5546: 5543: 5541: 5538: 5536: 5533: 5532: 5530: 5520: 5515: 5510: 5506: 5492: 5488: 5487: 5482: 5479: 5475: 5474: 5469: 5466: 5462: 5461: 5456: 5453: 5449: 5448: 5443: 5440: 5436: 5435: 5430: 5427: 5423: 5422: 5417: 5414: 5410: 5409: 5404: 5403: 5401: 5397: 5391: 5388: 5386: 5383: 5381: 5378: 5376: 5373: 5371: 5368: 5367: 5365: 5361: 5355: 5352: 5350: 5349:Enzyme family 5347: 5345: 5342: 5340: 5337: 5336: 5334: 5330: 5324: 5321: 5319: 5316: 5314: 5313:Cooperativity 5311: 5309: 5306: 5305: 5303: 5299: 5293: 5290: 5288: 5285: 5283: 5280: 5278: 5275: 5273: 5272:Oxyanion hole 5270: 5268: 5265: 5263: 5260: 5258: 5255: 5254: 5252: 5248: 5244: 5237: 5232: 5230: 5225: 5223: 5218: 5217: 5214: 5198: 5195: 5193: 5190: 5188: 5185: 5184: 5182: 5179: 5175: 5169: 5168: 5163: 5162: 5160: 5157: 5153: 5147: 5146: 5141: 5140: 5138: 5136: 5132: 5128: 5122: 5121: 5116: 5115: 5113: 5111: 5107: 5103: 5100: 5097: 5089: 5084: 5074: 5071: 5070: 5068: 5064: 5058: 5055: 5053: 5050: 5048: 5045: 5043: 5040: 5039: 5037: 5033: 5030: 5027: 5023: 5013: 5010: 5007: 5003: 5000: 4999: 4997: 4993: 4987: 4984: 4983: 4981: 4979: 4975: 4969: 4966: 4964: 4961: 4960: 4958: 4956: 4952: 4946: 4943: 4941: 4938: 4937: 4935: 4933: 4928: 4924: 4914: 4911: 4909: 4906: 4904: 4901: 4899: 4896: 4892: 4889: 4887: 4884: 4882: 4879: 4878: 4877: 4874: 4870: 4867: 4866: 4865: 4862: 4860: 4857: 4855: 4852: 4850: 4847: 4845: 4842: 4840: 4837: 4835: 4832: 4831: 4829: 4827: 4823: 4815: 4812: 4811: 4810: 4807: 4804: 4803: 4798: 4795: 4793: 4790: 4788: 4785: 4784: 4782: 4779: 4775: 4772: 4770: 4767: 4765: 4762: 4760: 4757: 4756: 4754: 4751: 4748: 4745: 4741: 4740: 4736: 4734: 4731: 4729: 4726: 4724: 4721: 4719: 4716: 4715: 4713: 4710: 4706: 4705: 4701: 4699: 4696: 4694: 4691: 4689: 4686: 4684: 4681: 4680: 4678: 4675: 4672: 4671: 4669: 4667: 4663: 4660: 4658: 4654: 4651: 4648: 4639: 4635: 4631: 4625: 4622: 4620: 4617: 4616: 4614: 4611: 4599: 4595: 4591: 4581: 4578: 4576: 4573: 4571: 4568: 4566: 4563: 4561: 4558: 4556: 4553: 4552: 4550: 4547: 4540: 4536: 4530: 4527: 4526: 4524: 4521: 4517: 4513: 4507: 4504: 4502: 4499: 4498: 4496: 4493: 4489: 4485: 4479: 4476: 4474: 4471: 4467: 4466:Class II PI 3 4464: 4462: 4459: 4458: 4457: 4454: 4452: 4449: 4447: 4444: 4442: 4441:Deoxycytidine 4439: 4437: 4434: 4432: 4429: 4427: 4424: 4422: 4419: 4417: 4414: 4410: 4409:ADP-thymidine 4407: 4406: 4405: 4402: 4400: 4397: 4395: 4392: 4388: 4385: 4383: 4380: 4378: 4375: 4373: 4370: 4368: 4365: 4364: 4363: 4360: 4358: 4355: 4351: 4348: 4347: 4346: 4343: 4341: 4338: 4336: 4333: 4332: 4330: 4327: 4323: 4319: 4316: 4313: 4305: 4301: 4295: 4290: 4286: 4282: 4275: 4270: 4268: 4263: 4261: 4256: 4255: 4252: 4240: 4239:Jacques Monod 4237: 4235: 4232: 4231: 4229: 4225: 4217: 4214: 4212: 4209: 4208: 4207: 4204: 4202: 4201:Translational 4199: 4195: 4192: 4190: 4187: 4185: 4182: 4181: 4180: 4177: 4175: 4172: 4168: 4165: 4163: 4160: 4159: 4158: 4155: 4151: 4148: 4147: 4146: 4143: 4142: 4140: 4138: 4134: 4124: 4121: 4119: 4116: 4114: 4111: 4109: 4106: 4105: 4103: 4099: 4093: 4090: 4088: 4085: 4083: 4080: 4079: 4077: 4073: 4070: 4068: 4064: 4054: 4051: 4049: 4046: 4044: 4041: 4039: 4036: 4034: 4031: 4030: 4028: 4026: 4022: 4016: 4013: 4011: 4008: 4006: 4003: 4002: 4000: 3996: 3990: 3987: 3985: 3982: 3980: 3977: 3976: 3974: 3970: 3967: 3965: 3964:Transcription 3961: 3953: 3950: 3948: 3945: 3943: 3940: 3939: 3938: 3935: 3931: 3927: 3923: 3920: 3919: 3918: 3917:Central dogma 3915: 3913: 3910: 3909: 3907: 3905: 3899: 3895: 3888: 3883: 3881: 3876: 3874: 3869: 3868: 3865: 3860: 3856: 3852: 3845: 3842: 3841: 3840: 3838: 3831: 3828: 3826: 3823: 3820: 3817: 3813: 3810: 3807: 3804: 3803: 3799: 3790: 3786: 3782: 3778: 3774: 3770: 3763: 3760: 3755: 3751: 3747: 3743: 3739: 3735: 3728: 3725: 3720: 3716: 3711: 3706: 3702: 3698: 3694: 3687: 3684: 3681: 3676: 3673: 3668: 3664: 3659: 3654: 3650: 3646: 3642: 3635: 3632: 3627: 3623: 3619: 3615: 3611: 3607: 3603: 3599: 3595: 3591: 3584: 3581: 3576: 3572: 3567: 3562: 3558: 3554: 3550: 3543: 3540: 3535: 3531: 3526: 3521: 3517: 3513: 3509: 3505: 3501: 3497: 3493: 3486: 3483: 3478: 3474: 3469: 3464: 3459: 3454: 3450: 3446: 3442: 3438: 3434: 3427: 3424: 3419: 3415: 3410: 3405: 3401: 3397: 3393: 3389: 3385: 3378: 3375: 3370: 3366: 3361: 3356: 3352: 3348: 3344: 3340: 3337:(1): e00399. 3336: 3332: 3328: 3321: 3318: 3313: 3309: 3305: 3301: 3297: 3293: 3289: 3285: 3281: 3277: 3273: 3266: 3263: 3258: 3254: 3249: 3244: 3240: 3236: 3232: 3228: 3224: 3220: 3216: 3209: 3207: 3203: 3198: 3194: 3189: 3184: 3180: 3176: 3172: 3168: 3164: 3157: 3154: 3149: 3145: 3140: 3135: 3131: 3127: 3123: 3116: 3113: 3108: 3104: 3100: 3096: 3092: 3088: 3080: 3077: 3072: 3068: 3063: 3058: 3054: 3050: 3046: 3042: 3038: 3031: 3028: 3023: 3019: 3015: 3011: 3008:(4): 186–94. 3007: 3003: 2996: 2993: 2988: 2984: 2980: 2976: 2972: 2968: 2961: 2958: 2953: 2949: 2945: 2941: 2937: 2933: 2925: 2922: 2917: 2913: 2908: 2903: 2899: 2895: 2891: 2887: 2883: 2876: 2873: 2868: 2864: 2860: 2856: 2851: 2846: 2842: 2838: 2834: 2830: 2826: 2819: 2816: 2811: 2807: 2802: 2797: 2793: 2789: 2785: 2778: 2775: 2770: 2766: 2761: 2756: 2752: 2748: 2744: 2740: 2736: 2729: 2726: 2721: 2717: 2713: 2711:9780125400626 2707: 2703: 2699: 2695: 2688: 2685: 2680: 2676: 2672: 2668: 2664: 2660: 2653: 2650: 2645: 2641: 2636: 2631: 2627: 2623: 2619: 2615: 2611: 2609: 2605: 2596: 2593: 2588: 2584: 2579: 2574: 2570: 2566: 2562: 2558: 2554: 2552: 2548: 2539: 2536: 2531: 2527: 2523: 2519: 2515: 2511: 2507: 2501: 2498: 2493: 2489: 2484: 2479: 2474: 2469: 2465: 2461: 2457: 2453: 2449: 2442: 2439: 2434: 2430: 2426: 2422: 2418: 2414: 2407: 2404: 2399: 2395: 2391: 2387: 2383: 2379: 2372: 2369: 2364: 2360: 2356: 2352: 2348: 2344: 2337: 2334: 2322: 2315: 2312: 2307: 2303: 2298: 2293: 2289: 2285: 2281: 2277: 2270: 2267: 2262: 2258: 2253: 2248: 2244: 2240: 2236: 2232: 2228: 2221: 2218: 2205: 2201: 2197: 2190: 2187: 2182: 2178: 2173: 2168: 2163: 2158: 2154: 2150: 2146: 2139: 2136: 2131: 2127: 2122: 2117: 2113: 2109: 2105: 2101: 2097: 2093: 2089: 2085: 2078: 2075: 2070: 2066: 2061: 2056: 2052: 2048: 2044: 2040: 2036: 2032: 2028: 2021: 2018: 2013: 2006: 2004: 2000: 1995: 1991: 1987: 1983: 1979: 1975: 1968: 1965: 1962: 1961: 1956: 1951: 1948: 1943: 1939: 1935: 1931: 1927: 1923: 1916: 1913: 1908: 1904: 1899: 1894: 1890: 1886: 1882: 1878: 1874: 1867: 1864: 1859: 1855: 1851: 1849:9780815344322 1845: 1841: 1834: 1831: 1826: 1822: 1817: 1812: 1807: 1802: 1798: 1794: 1790: 1783: 1781: 1779: 1777: 1775: 1771: 1766: 1762: 1757: 1752: 1748: 1744: 1740: 1733: 1730: 1725: 1721: 1716: 1711: 1707: 1703: 1699: 1695: 1691: 1684: 1681: 1675: 1672: 1659: 1654: 1650: 1646: 1639: 1636: 1633: 1628: 1625: 1620: 1616: 1612: 1608: 1604: 1600: 1595: 1590: 1586: 1582: 1578: 1574: 1567: 1565: 1563: 1561: 1557: 1552: 1548: 1544: 1540: 1536: 1532: 1524: 1520: 1516: 1512: 1508: 1504: 1500: 1496: 1489: 1487: 1485: 1483: 1479: 1472: 1468: 1465: 1463: 1460: 1459: 1455: 1453: 1447: 1443: 1440: 1436: 1433: 1429: 1426: 1422: 1421: 1420: 1414: 1412: 1410: 1406: 1402: 1398: 1394: 1386: 1384: 1382: 1378: 1374: 1373:dsRNA viruses 1370: 1366: 1361: 1359: 1354: 1351: 1347: 1345: 1342: 1341:bacteriophage 1338: 1334: 1330: 1325: 1322: 1318: 1310: 1306: 1300: 1293: 1291: 1287: 1285: 1281: 1277: 1272: 1268: 1263: 1261: 1260: 1255: 1254: 1249: 1248: 1244: 1239: 1232: 1230: 1228: 1224: 1219: 1217: 1212: 1203: 1199: 1195: 1192: 1189: 1185: 1182: 1179: 1175: 1172:found in the 1171: 1168:5S and other 1167: 1163: 1159: 1156: 1153: 1149: 1145: 1141: 1137: 1134: 1131: 1127: 1123: 1120: 1119: 1117: 1115: 1108: 1104: 1099: 1092: 1090: 1088: 1080: 1077: 1073: 1070: 1067: 1063: 1060: 1056: 1053: 1052: 1051: 1049: 1044: 1042: 1038: 1034: 1026: 1024: 1021: 1013: 1011: 1009: 1003: 1001: 997: 991: 983: 981: 978: 975: 967: 956:+ NTP → (NMP) 951: 950: 949: 947: 942: 935: 931: 930: 924: 916: 909: 907: 905: 899: 896: 887: 885: 882: 878: 872: 870: 866: 862: 858: 854: 849: 845: 837: 834: 826: 824: 822: 818: 814: 812: 801: 797: 794: 791: 788: 787:Ribosomal RNA 785: 783: 779: 775: 771: 768: 767: 765: 761: 760:ribosomal RNA 757: 753: 750: 747: 743: 739: 738:Messenger RNA 736: 735: 734: 731: 729: 725: 721: 717: 713: 712:complementary 709: 704: 702: 698: 693: 689: 685: 677: 673: 669: 665: 661: 656: 649: 647: 645: 641: 637: 632: 630: 626: 622: 617: 615: 611: 564: 560: 552: 542: 538: 533: 527: 515: 509: 505: 501: 498: 495: 491: 488:found in the 487: 483: 480: 477: 473: 470: 467: 463: 459: 456: 455: 453: 450: 448: 444: 440: 436: 432: 428: 424: 420: 416: 412: 404: 401: 397: 396:Catalytic RNA 394: 391: 388: 385: 382: 379: 378:Ribosomal RNA 376: 373: 369: 365: 361: 357: 354: 351: 350: 349: 347: 343: 342:messenger RNA 339: 334: 332: 328: 324: 320: 316: 312: 308: 307:transcription 304: 300: 295: 293: 289: 285: 281: 277: 273: 269: 265: 261: 252: 240: 237: 235: 231: 228: 225: 223: 219: 216: 213: 211: 207: 202: 198: 195: 191: 188: 186: 185:Gene Ontology 182: 179: 176: 173: 170: 167: 163: 160: 157: 155: 151: 148: 145: 143: 139: 136: 133: 131: 127: 124: 123:NiceZyme view 121: 119: 115: 112: 109: 107: 103: 100: 97: 95: 91: 86: 83: 80: 78: 74: 71: 68: 66: 62: 57: 50: 45: 40: 35: 30: 19: 5486:Translocases 5483: 5470: 5457: 5444: 5431: 5421:Transferases 5418: 5405: 5262:Binding site 5164: 5142: 5117: 4833: 4825: 4738: 4703: 4461:Class I PI 3 4426:Pantothenate 4297:2.7.1-2.7.4: 4281:Transferases 4216:irreversible 4101:Key elements 4009: 3998:Key elements 3912:Genetic code 3902:Introduction 3834: 3772: 3769:Biochemistry 3768: 3762: 3737: 3733: 3727: 3700: 3696: 3686: 3675: 3648: 3644: 3634: 3593: 3589: 3583: 3556: 3552: 3542: 3499: 3495: 3485: 3440: 3436: 3426: 3391: 3387: 3377: 3334: 3330: 3320: 3279: 3275: 3265: 3222: 3218: 3170: 3166: 3156: 3129: 3125: 3115: 3090: 3086: 3079: 3044: 3040: 3030: 3005: 3001: 2995: 2970: 2966: 2960: 2935: 2931: 2924: 2889: 2885: 2875: 2832: 2828: 2818: 2791: 2787: 2777: 2742: 2738: 2728: 2693: 2687: 2662: 2658: 2652: 2617: 2613: 2607: 2603: 2595: 2560: 2556: 2550: 2546: 2538: 2513: 2509: 2500: 2455: 2451: 2441: 2416: 2412: 2406: 2381: 2377: 2371: 2346: 2342: 2336: 2324:. Retrieved 2314: 2279: 2275: 2269: 2237:(1): 20–28. 2234: 2230: 2220: 2208:. Retrieved 2199: 2189: 2152: 2148: 2138: 2095: 2091: 2082:Goldman SR, 2077: 2034: 2030: 2020: 2011: 1977: 1973: 1967: 1958: 1950: 1925: 1921: 1915: 1880: 1876: 1866: 1839: 1833: 1796: 1793:PLOS Biology 1792: 1746: 1742: 1732: 1697: 1693: 1683: 1674: 1662:. Retrieved 1648: 1638: 1627: 1576: 1572: 1537:(1): 89–97. 1534: 1530: 1501:(2): 85–98. 1498: 1494: 1451: 1418: 1415:Purification 1405:Severo Ochoa 1390: 1362: 1348: 1326: 1315: 1288: 1279: 1275: 1270: 1264: 1257: 1251: 1245: 1236: 1223:mitochondria 1220: 1215: 1211:chloroplasts 1208: 1186:synthesizes 1160:synthesizes 1112: 1084: 1045: 1030: 1017: 1004: 993: 979: 971: 943: 939: 929:T. aquaticus 927: 900: 895:"scrunching" 891: 881:Supercoiling 873: 852: 847: 844:sigma factor 841: 810: 807: 770:Transfer RNA 756:transfer RNA 732: 705: 696: 681: 633: 618: 607: 532:T. aquaticus 531: 451: 443:mitochondria 439:chloroplasts 408: 353:Transfer RNA 335: 296: 279: 275: 271: 267: 263: 257: 111:BRENDA entry 29: 5257:Active site 5012:Transposase 5002:Recombinase 4647:-nucleoside 4473:Sphingosine 4067:Translation 3904:to genetics 2794:(1): 1–11. 1928:: 499–518. 1401:Nobel Prize 1350:B. subtilis 1271:S. shibatae 1209:Eukaryotic 1071:α (α and α) 984:Termination 782:translation 778:polypeptide 776:to growing 774:amino acids 764:translation 758:(tRNA) and 728:terminators 720:nucleotides 716:nucleotides 664:DNA strands 621:prokaryotes 372:translation 364:polypeptide 362:to growing 360:amino acids 344:(mRNA); or 303:nucleotides 99:IntEnz view 59:Identifiers 5529:Categories 5460:Isomerases 5434:Hydrolases 5301:Regulation 4814:Telomerase 4657:Polymerase 4431:Mevalonate 4394:Riboflavin 4285:phosphorus 4211:reversible 4174:lac operon 4150:imprinting 4145:Epigenetic 4137:Regulation 4092:Eukaryotic 4038:5' capping 3989:Eukaryotic 2506:Ebright RH 2084:Ebright RH 1473:References 1439:DNA column 1381:poliovirus 1379:, such as 1200:-directed 1190:in plants. 1170:small RNAs 1114:Eukaryotes 1103:α-amanitin 1093:Eukaryotes 996:rho factor 944:Aspartyl ( 926:RNAP from 910:Elongation 838:Initiation 831:See also: 724:dystrophin 668:RNA strand 486:small RNAs 431:eukaryotes 346:non-coding 331:eukaryotes 327:elongation 294:template. 168:structures 135:KEGG entry 82:9014-24-8 5339:EC number 5006:Integrase 4930:3' to 5' 4575:Guanylate 4570:Uridylate 4560:Adenylate 4404:Thymidine 4399:Shikimate 4082:Bacterial 3979:Bacterial 3859:IPR011773 3502:: 15774. 3312:205235881 2867:206507767 2413:Biochimie 1960:IPR011260 1858:887605755 1589:CiteSeerX 1269:) in the 1243:halophile 1148:microRNAs 1142:and most 934:magnesium 813:synthesis 793:Micro RNA 746:ribosomes 708:promoters 644:magnesium 636:cofactors 608:The 2006 566:​). 544:​). 516:Structure 413:and many 411:organisms 387:Micro RNA 321:called a 282:), is an 88:Databases 5550:EC 2.7.7 5363:Kinetics 5287:Cofactor 5250:Activity 4940:RNase PH 4548:acceptor 4529:Creatine 4522:acceptor 4494:acceptor 4436:Pyruvate 4421:Glycerol 4382:Platelet 4357:Galacto- 4328:acceptor 4194:microRNA 4108:Ribosome 4087:Archaeal 4043:Splicing 4015:Promoter 3984:Archaeal 3928: → 3924: → 3855:InterPro 3667:16230341 3626:42526536 3618:12016304 3575:31103775 3534:28585540 3477:31506349 3418:28701329 3369:27557794 3304:24153184 3257:18235446 3148:17697097 3107:20701995 3071:21949211 3022:23246438 2987:25596450 2952:10601874 2916:19377477 2859:15692015 2769:15372072 2679:16908155 2608:Anabaena 2606:gene of 2530:11124018 2433:17629387 2398:27371117 2363:12213656 2326:26 March 2306:19914059 2261:22982365 2204:Archived 2181:15610738 2130:19443781 2069:17110577 1955:InterPro 1942:11018136 1907:10500100 1825:19419240 1765:10499798 1724:11118218 1664:25 March 1551:11839495 1523:30004345 1515:21233849 1456:See also 1353:prophage 1312:​) 1130:ribosome 1033:bacteria 1027:Bacteria 968:Fidelity 821:helicase 800:Ribozyme 650:Function 619:In most 464:(35S in 423:bacteria 400:ribozyme 299:helicase 239:proteins 227:articles 215:articles 172:RCSB PDB 32:Compare 5545:Enzymes 5519:Biology 5473:Ligases 5243:Enzymes 4891:PrimPol 4876:Primase 4350:Hepatic 4345:Fructo- 3947:RNA→DNA 3942:RNA→RNA 3930:Protein 3825:2.7.7.6 3789:2261443 3754:2358436 3719:3525543 3598:Bibcode 3590:Science 3525:5467207 3504:Bibcode 3468:6765235 3445:Bibcode 3409:5584312 3360:5300874 3339:Bibcode 3284:Bibcode 3248:2805805 3227:Bibcode 3197:4940048 3188:1176638 3062:3252157 2907:2674513 2837:Bibcode 2829:Science 2810:8444147 2720:9932453 2644:1904436 2587:6287430 2547:E. coli 2492:9751740 2460:Bibcode 2252:3545073 2210:8 March 2121:2718712 2100:Bibcode 2092:Science 2060:2754787 2039:Bibcode 2031:Science 1994:1776168 1957::  1816:2675907 1619:1624391 1611:9419244 1581:Bibcode 1467:Primase 1448:column. 1387:History 1294:Viruses 1238:Archaea 1233:Archaea 1216:E. coli 1178:cytosol 1174:nucleus 853:E. coli 811:de novo 625:E. coli 494:cytosol 490:nucleus 427:archaea 415:viruses 389:(miRNA) 370:during 340:, i.e. 290:from a 194:QuickGO 159:profile 142:MetaCyc 77:CAS no. 70:2.7.7.6 5505:Portal 5447:Lyases 5178:2.7.13 5156:2.7.12 5131:2.7.11 5106:2.7.10 4945:PNPase 4913:PNPase 4869:POLRMT 4864:ssRNAP 4377:Muscle 4340:Gluco- 4304:kinase 3839:copy) 3818:(MeSH) 3787:  3752:  3717:  3665:  3624:  3616:  3573:  3532:  3522:  3475:  3465:  3416:  3406:  3367:  3357:  3310:  3302:  3276:Nature 3255:  3245:  3219:Nature 3195:  3185:  3146:  3105:  3069:  3059:  3020:  2985:  2950:  2914:  2904:  2865:  2857:  2808:  2767:  2760:524334 2757:  2718:  2708:  2677:  2642:  2635:207958 2632:  2585:  2578:320776 2575:  2528:  2490:  2480:  2431:  2396:  2361:  2304:  2259:  2249:  2179:  2128:  2118:  2067:  2057:  1992:  1940:  1905:  1898:317019 1895:  1856:  1846:  1823:  1813:  1763:  1722:  1715:305883 1712:  1617:  1609:  1591:  1549:  1521:  1513:  1444:By an 1395:, and 1329:POLRMT 1267:POLR2I 1227:POLRMT 848:before 827:Action 676:5′ end 672:3′ end 599:  593:  587:  581:  575:  435:phages 429:, and 380:(rRNA) 355:(tRNA) 338:coding 284:enzyme 272:RNApol 222:PubMed 204:Search 190:AmiGO 178:PDBsum 118:ExPASy 106:BRENDA 94:IntEnz 65:EC no. 5399:Types 5026:2.7.8 4995:Other 4634:2.7.7 4594:2.7.6 4539:2.7.4 4516:2.7.3 4488:2.7.2 4372:Liver 4335:Hexo- 4322:2.7.1 4075:Types 3972:Types 3622:S2CID 3394:(3). 3308:S2CID 2863:S2CID 2604:rpoC1 2483:21715 1615:S2CID 1519:S2CID 1437:By a 1423:By a 1198:siRNA 1188:siRNA 1162:tRNAs 1144:snRNA 1140:mRNAs 1087:sigma 952:(NMP) 508:siRNA 466:yeast 154:PRIAM 5491:list 5484:EC7 5478:list 5471:EC6 5465:list 5458:EC5 5452:list 5445:EC4 5439:list 5432:EC3 5426:list 5419:EC2 5413:list 5406:EC1 5165:see 5143:see 5118:see 4492:COOH 4291:2.7) 3853:and 3851:Pfam 3806:DNAi 3785:PMID 3750:PMID 3715:PMID 3663:PMID 3614:PMID 3571:PMID 3530:PMID 3473:PMID 3414:PMID 3365:PMID 3300:PMID 3253:PMID 3193:PMID 3144:PMID 3103:PMID 3067:PMID 3018:PMID 2983:PMID 2971:1847 2948:PMID 2912:PMID 2855:PMID 2806:PMID 2765:PMID 2716:PMID 2706:ISBN 2675:PMID 2640:PMID 2583:PMID 2551:rpoC 2526:PMID 2488:PMID 2429:PMID 2394:PMID 2359:PMID 2347:1577 2328:2019 2302:PMID 2257:PMID 2235:1829 2212:2017 2177:PMID 2126:PMID 2065:PMID 1990:PMID 1938:PMID 1903:PMID 1854:OCLC 1844:ISBN 1821:PMID 1761:PMID 1743:Cell 1720:PMID 1666:2022 1607:PMID 1547:PMID 1511:PMID 1371:and 1335:and 1309:1MSW 1256:and 1225:use 1176:and 1166:rRNA 1146:and 1126:rRNA 1066:rpoB 1039:and 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Index

DNA-dependent RNA polymerase
RNA-dependent RNA polymerase

EC no.
2.7.7.6
CAS no.
9014-24-8
IntEnz
IntEnz view
BRENDA
BRENDA entry
ExPASy
NiceZyme view
KEGG
KEGG entry
MetaCyc
metabolic pathway
PRIAM
profile
PDB
RCSB PDB
PDBe
PDBsum
Gene Ontology
AmiGO
QuickGO
PMC
articles
PubMed
articles

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