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  Structure of eukaryotic RNA polymerases.

Cramer, P., Armache, K. J., Baumli, S., Benkert, S., Brueckner, F., Buchen, C., et al. (2008). Structure of eukaryotic RNA polymerases. Annual Reviews of Biophysics, 37, 337-352. doi:10.1146/annurev.biophys.37.032807.130008.

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Cramer, P.1, Author           
Armache, K. J., Author
Baumli, S., Author
Benkert, S., Author
Brueckner, F., Author
Buchen, C., Author
Damsma, G. E., Author
Dengl, S., Author
Geiger, S. R., Author
Jasiak, A. J., Author
Jawhari, A., Author
Jennebach, S., Author
Kamenski, T., Author
Kettenberger, H., Author
Kuhn, C. D., Author
Lehmann, E., Author
Leike, K., Author
Sydow, J. F., Author
Vannini, A., Author
Affiliations:
1Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              

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 Abstract: 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.

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Language(s): eng - English
 Dates: 2008-02-072008-06
 Publication Status: Issued
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 Rev. Type: Peer
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Title: Annual Reviews of Biophysics
Source Genre: Journal
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Pages: - Volume / Issue: 37 Sequence Number: - Start / End Page: 337 - 352 Identifier: -