Structure of eukaryotic RNA polymerases

The eukaryotic RNA polymerases Pol I, Pol II, and Pol III are the central multiprotein machines that synthesize ribosomal, messenger, and transfer RNA, respectively. Here we provide a catalog of available structural information for these three enzymes. Most structural data have been accumulated for...

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Bibliographic Details
Published in:	Annual review of biophysics Vol. 37; no. 1; pp. 337 - 352
Main Authors:	Cramer, P, Armache, K-J, Baumli, S, Benkert, S, Brueckner, F, Buchen, C, Damsma, G E, Dengl, S, Geiger, S R, Jasiak, A J, Jawhari, A, Jennebach, S, Kamenski, T, Kettenberger, H, Kuhn, C-D, Lehmann, E, Leike, K, Sydow, J F, Vannini, A
Format:	Journal Article
Language:	English
Published:	United States 01-01-2008
Subjects:	Animals DNA-Directed RNA Polymerases - chemistry DNA-Directed RNA Polymerases - genetics DNA-Directed RNA Polymerases - ultrastructure Enzyme Activation Humans Models, Chemical Models, Genetic Models, Molecular RNA - biosynthesis RNA - chemistry RNA - genetics Transcription, Genetic - genetics
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Summary:	The eukaryotic RNA polymerases Pol I, Pol II, and Pol III are the central multiprotein machines that synthesize ribosomal, messenger, and transfer RNA, respectively. Here we provide a catalog of available structural information for these three enzymes. Most structural data have been accumulated for Pol II and its functional complexes. These studies have provided insights into many aspects of the transcription mechanism, including initiation at promoter DNA, elongation of the mRNA chain, tunability of the polymerase active site, which supports RNA synthesis and cleavage, and the response of Pol II to DNA lesions. Detailed structural studies of Pol I and Pol III were reported recently and showed that the active center region and core enzymes are similar to Pol II and that strong structural differences on the surfaces account for gene class-specific functions.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1
ISSN:	1936-122X 1936-1238
DOI:	10.1146/annurev.biophys.37.032807.130008