333:
344:
441:
250:
621:
654:, which is a cap-independent method of translational activation. Instead of building up a complex at the 5′ cap, the IRES allows for direct binding of the ribosomal complexes to the transcript to begin translation. The IRES enables the viral transcript to translate more efficiently due to the lack of needing a preinitation complex, allowing the virus to replicate quickly.
40:
457:
567:
The translation of the protein within the main ORF after a uORF sequence has been translated is known as reinitiation. The process of reinitiation is known to reduce the translation of the ORF protein. Control of protein regulation is determined by the distance between the uORF and the first codon in
1055:
Akulich, Kseniya A.; Andreev, Dmitry E.; Terenin, Ilya M.; Smirnova, Victoria V.; Anisimova, Aleksandra S.; Makeeva, Desislava S.; Arkhipova, Valentina I.; Stolboushkina, Elena A.; Garber, Maria B.; Prokofjeva, Maria M.; Spirin, Pavel V.; Prassolov, Vladimir S.; Shatsky, Ivan N.; Dmitriev, Sergey E.
912:
Rhind, Nicholas; Chen, Zehua; Yassour, Moran; Thompson, Dawn A.; Haas, Brian J.; Habib, Naomi; Wapinski, Ilan; Roy, Sushmita; Lin, Michael F.; Heiman, David I.; Young, Sarah K.; Furuya, Kanji; Guo, Yabin; Pidoux, Alison; Chen, Huei Mei; Robbertse, Barbara; Goldberg, Jonathan M.; Aoki, Keita; Bayne,
525:
from the binding of IRP1 and IRP2 to the IRE. When iron is high, then the two iron-regulatory proteins do not bind as strongly and allow proteins to be expressed that have a role in iron concentration control. This function has gained some interest after it was revealed that the translation of
568:
the main ORF. A uORF has been found to increase reinitiation with the longer distance between its uAUG and the start codon of the main ORF, which indicates that the ribosome needs to reacquire translation factors before it can carry out translation of the main protein. For example,
560:(uORF). These elements are fairly common, occurring in 35–49% of all human genes. A uORF is a coding sequence located in the 5′ UTR located upstream of the coding sequences initiation site. These uORFs contain their own initiation codon, known as an upstream AUG (uAUG). This
428:
gene. The protein SXL attaches to an intron segment located within the 5′ UTR segment of the primary transcript, which leads to the inclusion of the intron after processing. This sequence allows the recruitment of proteins that bind simultaneously to both the 5′ and
236:
of life accept and translate such mRNAs. Such sequences are naturally found in all three domains of life. Humans have many pressure-related genes under a 2–3 nucleotide leader. Mammals also have other types of ultra-short leaders like the
194:(usually AUG) of the coding region. In prokaryotes, the length of the 5′ UTR tends to be 3–10 nucleotides long, while in eukaryotes it tends to be anywhere from 100 to several thousand nucleotides long. For example, the
913:
Elizabeth H.; Berlin, Aaron M.; Desjardins, Christopher A.; Dobbs, Edward; Dukaj, Livio; Fan, Lin; Fitzgerald, Michael G.; French, Courtney; Gujja, Sharvari; Hansen, Klavs; Keifenheim, Dan; Levin, Joshua Z. (2011).
516:
Iron levels in cells are maintained by translation regulation of many proteins involved in iron storage and metabolism. The 5′ UTR has the ability to form a hairpin loop secondary structure (known as the
564:
can be scanned for by ribosomes and then translated to create a product, which can regulate the translation of the main protein coding sequence or other uORFs that may exist on the same transcript.
820:
Cenik, Can; Chua, Hon Nian; Zhang, Hui; Tarnawsky, Stefan P.; Akef, Abdalla; Derti, Adnan; Tasan, Murat; Moore, Melissa J.; Palazzo, Alexander F.; Roth, Frederick P. (2011). Snyder, Michael (ed.).
574:
regulation is performed by two uORFs further upstream, named uORF1 and uORF2, which contain three amino acids and fifty-nine amino acids, respectively. The location of uORF2 overlaps with the
1465:
Rogers, Jack T.; Bush, Ashley I.; Cho, Hyan-Hee; Smith, Deborah H.; Thomson, Andrew M.; Friedlich, Avi L.; Lahiri, Debomoy K.; Leedman, Peter J.; Huang, Xudong; Cahill, Catherine M. (2008).
385:
In both domains, genes without Shine–Dalgarno sequences are also translated in a less understood manner. A requirement seems to be a lack of secondary structure near the initiation codon.
382:
is less understood. SD sequences are much rarer, and the initiation factors have more in common with eukaryotic ones. There is no homolog of bacterial IF3. Some mRNAs are leaderless.
217:
only has seven nucleotides in its 5′ UTR. The differing sizes are likely due to the complexity of the eukaryotic regulation which the 5′ UTR holds as well as the larger
1289:
590:
ribosome will bypass uORF2 because of a decrease in concentration of eIF2-TC, which means the ribosome does not acquire one in time to translate uORF2. Instead,
686:
sites are located close to a small intron that is spliced in males, but kept in females through splicing inhibition. This splicing inhibition is maintained by
1467:"Iron and the translation of the amyloid precursor protein (APP) and ferritin mRNAs: Riboregulation against neural oxidative damage in Alzheimer's disease"
433:, not allowing translation proteins to assemble. However, it has also been noted that SXL can also repress translation of RNAs that do not contain a
521:
or IRE) that is recognized by iron-regulatory proteins (IRP1 and IRP2). In low levels of iron, the ORF of the target mRNA is blocked as a result of
729:
254:
1414:
988:
896:
1430:
Kozak, Marilyn (2008). "Faulty old ideas about translational regulation paved the way for current confusion about how microRNAs function".
1354:
Araujo, Patricia R.; Yoon, Kihoon; Ko, Daijin; Smith, Andrew D.; Qiao, Mei; Suresh, Uthra; Burns, Suzanne C.; Penalva, Luiz O. F. (2012).
364:
414:
bind the 5′ UTR, which limits the rate at which translational initiation can occur. However, this is not the only regulatory step of
1265:
218:
320:
are one such secondary structure that can be located within the 5′ UTR. These secondary structures also impact the regulation of
313:
145:
1305:"Comparative genomic analysis of translation initiation mechanisms for genes lacking the Shine-Dalgarno sequence in prokaryotes"
719:
531:
113:
651:
642:
625:
613:
289:
822:"Genome Analysis Reveals Interplay between 5′UTR Introns and Nuclear mRNA Export for Secretory and Mitochondrial Genes"
270:
606:
The nucleotides of an uORF may code for a codon that leads to a highly structured mRNA, causing the ribosome to stall.
551:
292:(uORFs) and upstream AUGs (uAUGs) and termination codons, which have a great impact on the regulation of translation (
586:
ORF, whose start codon is located within uORF2. This leads to its repression. However, during stress conditions, the
1213:
Benelli, D; Londei, P (January 2011). "Translation initiation in
Archaea: conserved and domain-specific features".
1248:
Hernández, Greco; Jagus, Rosemary (2016-08-10). "Evolution of
Translational Initiation: From Archaea to Eukarya".
527:
200:
556:
Another form of translational regulation in eukaryotes comes from unique elements on the 5′ UTR called upstream
1738:
278:
183:
59:
371:, bind to the Shine–Dalgarno (SD) sequence of the 5′ UTR. This then recruits many other proteins, such as the
160:
156:
773:"RNA Binding Protein Sex-Lethal (Sxl) and Control of Drosophila Sex Determination and Dosage Compensation"
539:
469:
415:
144:
of the mRNA. In many organisms, however, the 5′ UTR is completely untranslated, instead forming a complex
71:
734:
578:
ORF. During normal conditions, the uORF1 is translated, and then translation of uORF2 occurs only after
518:
511:
372:
368:
321:
266:
258:
121:
332:
375:, which allows for translation to begin. Each of these steps regulates the initiation of translation.
343:
265:
The elements of a eukaryotic and prokaryotic 5′ UTR differ greatly. The prokaryotic 5′ UTR contains a
1069:
926:
707:
424:
sometimes serve to prevent the pre-initiation complex from forming. An example is regulation of the
421:
238:
1283:
1146:
1006:"Ribosomes bind leaderless mRNA in Escherichia coli through recognition of their 5'-terminal AUG"
557:
678:
398:
The regulation of translation in eukaryotes is more complex than in prokaryotes. Initially, the
1709:
1660:
1596:
1547:
1496:
1447:
1410:
1387:
1336:
1271:
1261:
1230:
1195:
1138:
1097:
1037:
984:
952:
892:
888:
881:
861:
843:
802:
440:
453:
Another important regulator of translation is the interaction between 3′ UTR and the 5′ UTR.
1699:
1691:
1650:
1640:
1586:
1578:
1537:
1527:
1486:
1478:
1439:
1377:
1367:
1326:
1316:
1253:
1222:
1185:
1177:
1128:
1087:
1077:
1027:
1017:
942:
934:
851:
833:
792:
784:
522:
233:
213:
117:
672:
582:-TC has been reacquired. Translation of the uORF2 requires that the ribosomes pass by the
141:
136:. While called untranslated, the 5′ UTR or a portion of it is sometimes translated into a
1073:
930:
249:
1704:
1679:
1655:
1628:
1591:
1566:
1491:
1466:
1382:
1355:
1331:
1304:
1190:
1165:
1092:
1057:
1032:
1005:
947:
914:
856:
821:
739:
495:
491:
478:
1542:
1515:
797:
772:
502:. However, it is important to note that this mechanism has been under great scrutiny.
17:
1727:
109:
1532:
1058:"Four translation initiation pathways employed by the leaderless mRNA in eukaryotes"
281:(ACCAUGG), which contains the initiation codon. The eukaryotic 5′ UTR also contains
277:
upstream from the initiation codon. In contrast, the eukaryotic 5′ UTR contains the
1733:
1150:
788:
434:
317:
1004:
Brock, JE; Pourshahian, S; Giliberti, J; Limbach, PA; Janssen, GR (October 2008).
602:
In addition to reinitiation, uORFs contribute to translation initiation based on:
1645:
838:
64:
1257:
620:
191:
151:
The 5′ UTR has been found to interact with proteins relating to metabolism, and
129:
1443:
465:
430:
403:
1695:
629:
609:
cis- and trans- regulation on translation of the main protein coding sequence.
348:
309:
300:
in eukaryotes. In humans, ~35% of all genes harbor introns within the 5′ UTR.
282:
274:
205:
187:
165:
133:
1275:
847:
498:
of the PolyA tail, which can recruit the translational machinery by means of
938:
698:
by increasing translation of a start codon located in a uORF in the 5′ UTR (
229:
1713:
1664:
1600:
1582:
1551:
1500:
1451:
1391:
1340:
1234:
1199:
1142:
1133:
1116:
1101:
1041:
956:
865:
806:
169:. Regulatory elements within 5′ UTRs have also been linked to mRNA export.
39:
1372:
476:
The closed-loop structure inhibits translation. This has been observed in
1514:
Mignone, Flavio; Gissi, Carmela; Liuni, Sabino; Pesole, Graziano (2002).
1321:
461:
360:
337:
1181:
1022:
1567:"Upstream open reading frames: Molecular switches in (patho)physiology"
1482:
1226:
647:
456:
444:
The various forms of mRNA and how each affects translational regulation
379:
297:
261:(iron response element), which are hairpin loops, regulate translation.
137:
1082:
77:
683:
499:
706:
outcompetes TIA-1 to a poly(U) region and prevents snRNP (a step in
482:, in which eIF4E bound to the 5′ cap interacts with Maskin bound to
140:
product. This product can then regulate the translation of the main
1252:. Hernández, Greco,, Jagus, Rosemary. Switzerland. pp. 61–79.
406:, which in turn recruits the ribosomal complex to the 5′ UTR. Both
744:
619:
561:
439:
411:
407:
399:
342:
331:
248:
125:
1629:"A perspective on mammalian upstream open reading frame function"
155:
within the 5′ UTR. In addition, this region has been involved in
724:
579:
570:
535:
487:
483:
45:
1250:
Evolution of the
Protein Synthesis Machinery and Its Regulation
983:. New York, New York: Garland Science Publishing. p. 397.
1356:"Before It Gets Started: Regulating Translation at the 5′ UTR"
1166:"Control of mammalian translation by mRNA structure near caps"
587:
1164:
Babendure, J. R.; Babendure, JL; Ding, JH; Tsien, RY (2006).
1115:
Bicknell AA, Cenik C, Chua HN, Roth FP, Moore MJ (Dec 2012).
1633:
676:
transcript is regulated by multiple binding sites for fly
224:
The 5′ UTR can also be completely missing, in the case of
887:. New York, New York: W.H. Freeman and Company. p.
915:"Comparative Functional Genomics of the Fission Yeasts"
494:, displacing the Maskin binding site, allowing for the
490:. This translational inhibition is lifted once CPEB is
1627:
Somers, Joanna; Pöyry, Tuija; Willis, Anne E. (2013).
1565:
Wethmar, Klaus; Smink, Jeske J.; Leutz, Achim (2010).
1303:
Nakagawa, S; Niimura, Y; Gojobori, T (20 April 2017).
468:
and 5′ UTR causing a circularization that regulates
1117:"Introns in UTRs: why we should stop ignoring them"
58:
53:
32:
1409:. Sunderland, MA: Sinauer Associates. p. 60.
880:
486:on the 3′ UTR, creating translationally inactive
120:. This region is important for the regulation of
974:
972:
970:
968:
966:
650:(as well as some eukaryotic) 5′ UTRs contain
538:, leading to a spontaneous increased risk of
8:
363:, the initiation of translation occurs when
48:in eukaryotic organism (specifically humans)
124:of a transcript by differing mechanisms in
1680:"Tricks an IRES uses to enslave ribosomes"
1288:: CS1 maint: location missing publisher (
777:Microbiology and Molecular Biology Reviews
296:). Unlike prokaryotes, 5′ UTRs can harbor
38:
1703:
1654:
1644:
1590:
1541:
1531:
1490:
1381:
1371:
1330:
1320:
1189:
1132:
1091:
1081:
1031:
1021:
946:
855:
837:
796:
682:at the 5′ UTR. In particular, these poly-
637:Internal ribosome entry sites and viruses
44:The general structure of the 5′ UTR of a
455:
771:Penalva, L. O. F.; Sanchez, L. (2003).
756:
730:Iron-responsive element-binding protein
700:see above for more information on uORFs
204:has a 2273 nucleotide 5′ UTR while the
1281:
534:to the IRE found in the 5′ UTR of its
75:
29:
710:) recruitment to the 5′ splice site.
221:that must form to begin translation.
7:
1622:
1620:
1618:
1616:
1614:
1612:
1610:
1360:Comparative and Functional Genomics
766:
764:
762:
760:
658:Role in transcriptional regulation
25:
394:Pre-initiation complex regulation
273:(AGGAGGU), which is usually 3–10
257:(iron regulatory protein) to and
1471:Biochemical Society Transactions
1215:Biochemical Society Transactions
783:(3): 343–59, table of contents.
694:will repress the translation of
328:Role in translational regulation
1533:10.1186/gb-2002-3-3-reviews0004
1516:"Untranslated regions of mRNAs"
720:Three prime untranslated region
789:10.1128/MMBR.67.3.343-359.2003
532:single-nucleotide polymorphism
347:The process of translation in
336:The process of translation in
1:
652:internal ribosome entry sites
437:, or more generally, 3′ UTR.
1678:Thompson, Sunnie R. (2012).
1646:10.1016/j.biocel.2013.04.020
839:10.1371/journal.pgen.1001366
643:Internal ribosome entry site
402:complex is recruited to the
290:upstream open reading frames
153:proteins translate sequences
1258:10.1007/978-3-319-39468-8_4
552:Upstream open reading frame
288:regulatory elements called
1755:
1444:10.1016/j.gene.2008.07.013
699:
640:
549:
530:may be disrupted due to a
509:
418:that involves the 5′ UTR.
293:
1696:10.1016/j.tim.2012.08.002
528:amyloid precursor protein
269:(RBS), also known as the
201:Schizosaccharomyces pombe
182:The 5′ UTR begins at the
148:to regulate translation.
70:
37:
27:Region of a messenger RNA
279:Kozak consensus sequence
184:transcription start site
159:regulation, such as the
112:(mRNA) that is directly
1405:Gilbert, Scott (2010).
939:10.1126/science.1203357
879:Lodish, Havery (2004).
316:often occur within it.
308:As the 5′ UTR has high
271:Shine–Dalgarno sequence
1684:Trends in Microbiology
1583:10.1002/bies.201000037
1309:Nucleic Acids Research
1134:10.1002/bies.201200073
883:Molecular Cell Biology
633:
546:uORFs and reinitiation
473:
449:Closed-loop regulation
445:
351:
340:
262:
219:pre-initiation complex
90:5′ untranslated region
72:Anatomical terminology
33:5′ untranslated region
18:5′ untranslated region
1407:Developmental Biology
735:Iron response element
670:Transcription of the
628:in the 5′ UTR of the
623:
519:iron response element
512:Iron response element
460:Interactions between
459:
443:
373:50S ribosomal subunit
369:30S ribosomal subunit
346:
335:
267:ribosome binding site
252:
108:) is the region of a
1526:(3): reviews0004.1.
1056:(28 November 2016).
708:alternative splicing
422:RNA-binding proteins
314:secondary structures
1373:10.1155/2012/475731
1182:10.1261/rna.2309906
1074:2016NatSR...637905A
1023:10.1261/rna.1089208
979:Brown, T.A (2007).
931:2011Sci...332..930R
558:open reading frames
540:Alzheimer's disease
506:Ferritin regulation
304:Secondary structure
192:initiation sequence
146:secondary structure
1483:10.1042/BST0361282
1322:10.1093/nar/gkx124
1227:10.1042/BST0390089
1062:Scientific Reports
634:
612:Interactions with
474:
446:
352:
341:
263:
253:The binding of an
1416:978-0-87893-384-6
1083:10.1038/srep37905
990:978-0-8153-4138-3
898:978-0-7167-4366-8
367:, along with the
173:General structure
102:transcript leader
86:
85:
81:
16:(Redirected from
1746:
1718:
1717:
1707:
1675:
1669:
1668:
1658:
1648:
1624:
1605:
1604:
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1535:
1511:
1505:
1504:
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1421:
1420:
1402:
1396:
1395:
1385:
1375:
1351:
1345:
1344:
1334:
1324:
1315:(7): 3922–3931.
1300:
1294:
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1287:
1279:
1245:
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1238:
1210:
1204:
1203:
1193:
1161:
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817:
811:
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800:
768:
690:. When present,
598:Other mechanisms
523:steric hindrance
226:leaderless mRNAs
214:Escherichia coli
190:(nt) before the
154:
118:initiation codon
78:edit on Wikidata
42:
30:
21:
1754:
1753:
1749:
1748:
1747:
1745:
1744:
1743:
1739:Gene expression
1724:
1723:
1722:
1721:
1677:
1676:
1672:
1639:(8): 1690–700.
1626:
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1608:
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1508:
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1211:
1207:
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1162:
1158:
1127:(12): 1025–34.
1114:
1113:
1109:
1054:
1053:
1049:
1016:(10): 2159–69.
1003:
1002:
998:
991:
978:
977:
964:
925:(6032): 930–6.
911:
910:
906:
899:
878:
877:
873:
832:(4): e1001366.
819:
818:
814:
770:
769:
758:
753:
716:
668:
660:
645:
639:
600:
594:is translated.
554:
548:
514:
508:
451:
396:
391:
357:
330:
306:
247:
180:
175:
152:
142:coding sequence
98:leader sequence
92:(also known as
82:
49:
28:
23:
22:
15:
12:
11:
5:
1752:
1750:
1742:
1741:
1736:
1726:
1725:
1720:
1719:
1690:(11): 558–66.
1670:
1606:
1577:(10): 885–93.
1557:
1520:Genome Biology
1506:
1457:
1422:
1415:
1397:
1346:
1295:
1266:
1240:
1205:
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1107:
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962:
904:
897:
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812:
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748:
747:
742:
740:Trans-splicing
737:
732:
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715:
712:
667:
661:
659:
656:
641:Main article:
638:
635:
618:
617:
610:
607:
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550:Main article:
547:
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510:Main article:
507:
504:
496:polymerization
492:phosphorylated
479:Xenopus laevis
450:
447:
395:
392:
390:
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378:Initiation in
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329:
326:
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198:transcript in
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84:
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68:
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2:
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1521:
1517:
1510:
1507:
1502:
1498:
1493:
1488:
1484:
1480:
1477:(6): 1282–7.
1476:
1472:
1468:
1461:
1458:
1453:
1449:
1445:
1441:
1438:(2): 108–15.
1437:
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1412:
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1401:
1398:
1393:
1389:
1384:
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239:TISU sequence
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232:of all three
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1221:(1): 89–93.
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1068:(1): 37905.
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624:An example
488:transcripts
470:translation
416:translation
355:Prokaryotes
322:translation
130:prokaryotes
122:translation
54:Identifiers
1728:Categories
751:References
666:transcript
630:Poliovirus
389:Eukaryotes
349:eukaryotes
310:GC content
275:base pairs
188:nucleotide
166:Drosophila
161:sex-lethal
134:eukaryotes
106:leader RNA
46:transcript
1571:BioEssays
1284:cite book
1276:956539514
1121:BioEssays
981:Genomes 3
848:1553-7404
702:). Also,
294:see below
230:Ribosomes
116:from the
1714:22944245
1665:23624144
1601:20726009
1552:11897027
1501:19021541
1452:18692553
1392:22693426
1341:28334743
1235:21265752
1200:16540693
1143:23108796
1102:27892500
1042:18755843
957:21511999
866:21533221
807:12966139
714:See also
462:proteins
361:bacteria
338:bacteria
245:Elements
163:gene in
114:upstream
1705:3479354
1656:7172355
1592:3045505
1492:2746665
1383:3368165
1366:: 1–8.
1332:5397173
1191:1440912
1151:5808466
1093:5124965
1070:Bibcode
1033:2553737
948:3131103
927:Bibcode
919:Science
857:3077370
380:Archaea
298:introns
286:-acting
234:domains
138:protein
126:viruses
65:D020121
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795:
684:uracil
632:genome
616:sites.
466:3′ UTR
431:3′ UTR
404:5′ cap
209:operon
178:Length
94:5′ UTR
1147:S2CID
745:UTRdb
673:msl-2
664:msl-2
648:Viral
562:codon
412:eIF4G
408:eIF4E
400:eIF4F
196:ste11
104:, or
76:[
1710:PMID
1661:PMID
1597:PMID
1548:PMID
1497:PMID
1448:PMID
1432:Gene
1411:ISBN
1388:PMID
1364:2012
1337:PMID
1290:link
1272:OCLC
1262:ISBN
1231:PMID
1196:PMID
1139:PMID
1098:PMID
1038:PMID
985:ISBN
953:PMID
893:ISBN
862:PMID
844:ISSN
803:PMID
725:UORF
696:msl2
626:IRES
614:IRES
592:ATF4
584:ATF4
580:eIF2
576:ATF4
571:ATF4
536:mRNA
500:PABP
484:CPEB
426:msl2
410:and
365:IF-3
132:and
88:The
60:MeSH
1734:RNA
1700:PMC
1692:doi
1651:PMC
1641:doi
1587:PMC
1579:doi
1538:PMC
1528:doi
1487:PMC
1479:doi
1440:doi
1436:423
1378:PMC
1368:doi
1327:PMC
1317:doi
1254:doi
1223:doi
1186:PMC
1178:doi
1170:RNA
1129:doi
1088:PMC
1078:doi
1028:PMC
1018:doi
1010:RNA
943:PMC
935:doi
923:332
889:113
852:PMC
834:doi
793:PMC
785:doi
704:Sxl
692:Sxl
688:Sxl
679:Sxl
588:40S
359:In
284:cis
259:IRE
255:IRP
211:in
207:lac
1730::
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