Abstract
Eukaryotic nuclei contain three different types of RNA polymerases (RNAPs), each consisting of 12–18 different subunits. The evolutionarily highly conserved RNAP subunit RPB5 is shared by all three enzymes and therefore represents a key structural/functional component of all eukaryotic RNAPs. Here we present the crystal structure of the RPB5 subunit from Saccharomyces cerevisiae . The bipartite structure includes a eukaryote-specific N-terminal domain and a C-terminal domain resembling the archaeal RNAP subunit H. RPB5 has been implicated in direct protein-protein contacts with transcription factor IIB, one of the components of the RNAP II basal transcriptional machinery, and gene-specific activator proteins, such as the hepatitis B virus transactivator protein X. The experimentally mapped regions of RPB5 involved in these interactions correspond to distinct and surface-exposed α-helical structures.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 26, 2002, 10:41 a.m.) |
Deposited | 3 years, 2 months ago (June 7, 2022, 12:49 a.m.) |
Indexed | 1 month, 2 weeks ago (July 11, 2025, 6:47 a.m.) |
Issued | 25 years, 2 months ago (June 6, 2000) |
Published | 25 years, 2 months ago (June 6, 2000) |
Published Online | 25 years, 2 months ago (June 6, 2000) |
Published Print | 25 years, 2 months ago (June 6, 2000) |
@article{Todone_2000, title={Crystal structure of RPB5, a universal eukaryotic RNA polymerase subunit and transcription factor interaction target}, volume={97}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.97.12.6306}, DOI={10.1073/pnas.97.12.6306}, number={12}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Todone, Flavia and Weinzierl, Robert O. J. and Brick, Peter and Onesti, Silvia}, year={2000}, month=jun, pages={6306–6310} }