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PMID: 9974391 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Conserved structures of mediator and RNA polymerase II holoenzyme.

Science (New York, N.Y.) ·Vol. 283 ·No. 5404 ·1999-02-12 ·Pages 985-7

Asturias FJ, Jiang YW, Myers LC, Gustafsson CM, Kornberg RD

Abstract

Single particles of the mediator of transcriptional regulation (Mediator) and of RNA polymerase II holoenzyme were revealed by electron microscopy and image processing. Mediator alone appeared compact, but at high pH or in the presence of RNA polymerase II it displayed an extended conformation. Holoenzyme contained Mediator in a fully extended state, partially enveloping the globular polymerase, with points of apparent contact in the vicinity of the polymerase carboxyl-terminal domain and the DNA-binding channel. A similarity in appearance and conformational behavior of yeast and murine complexes indicates a conservation of Mediator structure among eukaryotes.

MeSH Terms
Animals DNA-Directed RNA Polymerases/chemistry,metabolism Fungal Proteins/chemistry,metabolism Holoenzymes/chemistry,metabolism Hydrogen-Ion Concentration Mice Microscopy, Electron Protein Conformation Protein Folding Temperature Trans-Activators/chemistry,metabolism Transcription Factors/chemistry,metabolism
Chemicals
Fungal Proteins Holoenzymes Trans-Activators Transcription Factors DNA-Directed RNA Polymerases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Asturias F J
Department of Structural Biology, Fairchild Building, Stanford University School of Medicine, Stanford, CA 94305, USA.
Jiang Y W
Myers L C
Gustafsson C M
Kornberg R D
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1999-02-12
Pages
985-7
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Grants
NIAID NIH HHS · AI21144 · United States
NIGMS NIH HHS · GM36659 · United States
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