RNA polymerase

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* [[Transcription and RNA Processing]].<br />
* [[Transcription and RNA Processing]].<br />
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'''RNA-dependent RNA polymerase''' or '''cap-snatching endonuclease''' catalyzes the replication of RNA from a RNA template<ref>PMID:12016304</ref>. An example is the '''Influenza virus RNA polymerase''' which is composed of 3 subunits. Subunit '''PA''' is involved in cap-snatching. Subunit '''PB1''' is involved in RNA synthesis. Subunit '''PB2''' is involved in RNA replication and transcription. It is implicated in endonuclease cleavage of RNA primers. <scene name='1qln/Rockets_steitz_colors/1'>View of the nucleic acid</scene> ([[1qln]]; blue: nontemplate strand; cyan: template strand; red:RNA).<br />
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'''RNA-dependent RNA polymerase''' or '''cap-snatching endonuclease''' or '''replicase''' catalyzes the replication of RNA from a RNA template<ref>PMID:12016304</ref>. An example is the '''Influenza virus RNA polymerase''' which is composed of 3 subunits. Subunit '''PA''' is involved in cap-snatching. Subunit '''PB1''' is involved in RNA synthesis. Subunit '''PB2''' is involved in RNA replication and transcription. It is implicated in endonuclease cleavage of RNA primers. <scene name='1qln/Rockets_steitz_colors/1'>View of the nucleic acid</scene> ([[1qln]]; blue: nontemplate strand; cyan: template strand; red:RNA).<br />
See also [[RNA-directed RNA polymerase]].<br />
See also [[RNA-directed RNA polymerase]].<br />
For RNA-dependent RNA polymerase from Hepatitis C virus - NS5B - see<br />
For RNA-dependent RNA polymerase from Hepatitis C virus - NS5B - see<br />

Revision as of 11:17, 5 November 2023

Yeast RNA polymerase II elongation complex C complexed with DNA and RNA and Zn+2 (grey) and Mg+2 (green) ions 3m3y. Subunit B1 (grey), B2 (green), B3 (pink), B9 (wheat), B11 (rust), ABC1 (magenta), ABC2 (cyan), ABC3 (red), ABC4 (aqua), ABC5 (blue) (PDB code 3m3y).

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References

  1. ↑ Cramer P, Armache KJ, Baumli S, Benkert S, Brueckner F, Buchen C, Damsma GE, Dengl S, Geiger SR, Jasiak AJ, Jawhari A, Jennebach S, Kamenski T, Kettenberger H, Kuhn CD, Lehmann E, Leike K, Sydow JF, Vannini A. Structure of eukaryotic RNA polymerases. Annu Rev Biophys. 2008;37:337-52. doi: 10.1146/annurev.biophys.37.032807.130008. PMID:18573085 doi:http://dx.doi.org/10.1146/annurev.biophys.37.032807.130008
  2. ↑ Comai L. Mechanism of RNA polymerase I transcription. Adv Protein Chem. 2004;67:123-55. PMID:14969726 doi:http://dx.doi.org/10.1016/S0065-3233(04)67005-7
  3. ↑ Hahn S. Structure and mechanism of the RNA polymerase II transcription machinery. Nat Struct Mol Biol. 2004 May;11(5):394-403. PMID:15114340 doi:http://dx.doi.org/10.1038/nsmb763
  4. ↑ Longo DL, Herbert V. Radioassay for serum and red cell folate. J Lab Clin Med. 1976 Jan;87(1):138-51. PMID:1452
  5. ↑ Frick DN, Richardson CC. DNA primases. Annu Rev Biochem. 2001;70:39-80. PMID:11395402 doi:http://dx.doi.org/10.1146/annurev.biochem.70.1.39
  6. ↑ Naue N, Beerbaum M, Bogutzki A, Schmieder P, Curth U. The helicase-binding domain of Escherichia coli DnaG primase interacts with the highly conserved C-terminal region of single-stranded DNA-binding protein. Nucleic Acids Res. 2013 Apr;41(8):4507-17. doi: 10.1093/nar/gkt107. Epub 2013 Feb, 20. PMID:23430154 doi:http://dx.doi.org/10.1093/nar/gkt107
  7. ↑ Ahlquist P. RNA-dependent RNA polymerases, viruses, and RNA silencing. Science. 2002 May 17;296(5571):1270-3. PMID:12016304 doi:http://dx.doi.org/10.1126/science.1069132
  8. ↑ Fukushi S, Kojima S, Takai R, Hoshino FB, Oka T, Takeda N, Katayama K, Kageyama T. Poly(A)- and primer-independent RNA polymerase of Norovirus. J Virol. 2004 Apr;78(8):3889-96. PMID:15047805

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