Primary Source |
[1] Chamberlin, M. (1977) In RNA Polymerase, eds. Losick, R. & Chamberlin, M. (Cold Spring Harbor Lab. Press, Plainview, NY), pp. 17–67. [2] Young, R. A. (1991) RNA polymerase II. Annu. Rev. Biochem. 60, 689–715. [3] Thurioux, P. & Sentenac, A. (1992) in The Molecular and Cellular Biology of the Yeast Saccharomyces: Gene Expression, eds. Jones, E. W., Pringle, J. R. & Broach, J. R. (Cold Spring Harbor Lab. Press, Plainview, NY), Vol. 2, pp. 1–48. [4] Archambault, J. & Friesen, J. D. (1993) Genetics of eukaryotic RNA polymerases I, II, and III. Microbiol. Rev. 57, 703–724. [5] Bell, S. D. & Jackson, S. P. (1998) Transcription in Archaea. Cold Spring Harbor Symp. Quant. Biol. 63, 41–51. [6] Zhang, G. et al., (1999) Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution. Cell 98, 811–824. [7] Cramer, P. et al., (2000) Architecture of RNA polymerase II and implications for the transcription mechanism. Science 288, 640–649.PubMed ID1883205, 8246845, 10384269, 10499798, 10784442
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Comments |
"The DNA-dependent RNA polymerase (RNAP) is central to all steps of the transcription cycle (primary sources 1–5). Bacterial, archaeal, and eukaryotic cellular RNAPs are large, multisubunit enzymes. Bacterial RNAP core enzyme consists of five subunits (ß', ß, a?, aII, and ?) and has a molecular mass of ˜0.35 MDa (primary sources 1, 6). Archaeal and eukaryotic RNAP core enzymes consist of 10 to 20 subunits and have molecular masses of 0.4–0.8 MDa (primary sources 3–5, 7)." |