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Opening and closing of the bacterial RNA polymerase clamp.

Chakraborty, Anirban
; 
Wang, Dongye
; 
Ebright, Yon W
; 
Korlann, You
; 
Kortkhonjia, Ekaterine
; 
Kim, Taiho
; 
Chowdhury, Saikat
; 
Wigneshweraraj, Sivaramesh
; 
Irschik, Herbert
; 
Jansen, Rolf
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Issue Date
2012-08-03
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Abstract
Using single-molecule fluorescence resonance energy transfer, we have defined bacterial RNA polymerase (RNAP) clamp conformation at each step in transcription initiation and elongation. We find that the clamp predominantly is open in free RNAP and early intermediates in transcription initiation but closes upon formation of a catalytically competent transcription initiation complex and remains closed during initial transcription and transcription elongation. We show that four RNAP inhibitors interfere with clamp opening. We propose that clamp opening allows DNA to be loaded into and unwound in the RNAP active-center cleft, that DNA loading and unwinding trigger clamp closure, and that clamp closure accounts for the high stability of initiation complexes and the high stability and processivity of elongation complexes.
Citation
Opening and closing of the bacterial RNA polymerase clamp. 2012, 337 (6094):591-5 Science
Affiliation
Howard Hughes Medical Institute, Waksman Institute, and Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ 08854, USA.
Publisher
Journal
Science (New York, N.Y.)
URI
http://hdl.handle.net/10033/246442
DOI
10.1126/science.1218716
PubMed ID
22859489
PubMed Central ID
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Article
Language
en
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ISSN
1095-9203
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Archived with thanks to Science (New York, N.Y.)
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publications of the research group of microbial drugs (MWIS)