RNA polymerase

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Contents


Function

RNA polymerase (RNAP, DNA primase, dnaG) catalyzes the addition of nucleotides to RNA during transcription.
DNA-dependent RNA polymerase catalyzes the transcription of RNA from a DNA template. The DNA-dependent eukaryote RNAP[1] are divided to
RNAP I (or Pol I) which transcribes ribosomal RNA[2];
RNAP II (or Pol II) transcribes DNA and most snRNA and microRNA[3]; See RNA Polymerase II.
RNAP III (or Pol III) transcribes tRNA and 5S ribosomal RNA[4].
DNA primase (DNAP) is RNAP which catalyzes the synthesis of the RNA primer which complements an ssDNA template and initiates DNA synthesis[5]. The large subunit of promase is called p58C.
dnaG is a bacterial DNA primase[6].
For DNA-dependent RNA polymerase see

RNA-dependent RNA polymerase or cap-snatching endonuclease or replicase catalyzes the replication of RNA from a RNA template[7]. 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. View of the nucleic acid (1qln; blue: nontemplate strand; cyan: template strand; red:RNA).
See also RNA-directed RNA polymerase.
For RNA-dependent RNA polymerase from Hepatitis C virus - NS5B - see

For RNA-dependent RNA polymerase from murine norovirus see

Poly(A) RNA polymerase catalyzes the addition of long poly(A) tails to mRNA without a template[8].

3D Structures of RNA polymerase

RNA polymerase 3D structures


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).

Drag the structure with the mouse to rotate

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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