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PMID: 9325110 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Two conformations of RNA polymerase II revealed by electron crystallography.

Journal of molecular biology ·Vol. 272 ·No. 4 ·1997-10-03 ·Pages 536-40

Asturias FJ, Meredith GD, Poglitsch CL, Kornberg RD

Abstract

A new two-dimensional crystal form of yeast RNA polymerase II was obtained in which the conformation of the enzyme appears "open", allowing entry of DNA, as required for the initiation of transcription. By contrast, a previous crystal form contained the enzyme in a "closed" conformation, appropriate for retention of DNA during RNA chain elongation. Interaction with two polymerase subunits, Rpb4 and Rpb7, favors the closed conformation, and binding of general transcription factor TFIIE may do so as well. The effect of Rpb4 and Rpb7, together with previous biochemical evidence, leads to the conclusion that the open to closed transition is a crucial step in the transcription initiation process.

MeSH Terms
Acetates Crystallography, X-Ray DNA, Fungal/metabolism Models, Molecular Protein Conformation RNA Polymerase II/chemistry,metabolism Saccharomyces cerevisiae/enzymology Transcription Factors/metabolism Transcription Factors, TFII
Chemicals
Acetates DNA, Fungal Transcription Factors Transcription Factors, TFII transcription factor TFIIE RNA Polymerase II ammonium acetate
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Asturias F J
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305-5400, USA.
Meredith G D
Poglitsch C L
Kornberg R D
Article Info
Journal
Journal of molecular biology
Abbr.
J Mol Biol
ISSN
0022-2836
Published
1997-10-03
Pages
536-40
Language
English
Region
England
NLM ID
2985088R
Subset
IM
Grants
NIAID NIH HHS · AI21144 · United States
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