2.50
Hdl Handle:
http://hdl.handle.net/10033/246442
Title:
Opening and closing of the bacterial RNA polymerase clamp.
Authors:
Chakraborty, Anirban; Wang, Dongye; Ebright, Yon W; Korlann, You; Kortkhonjia, Ekaterine; Kim, Taiho; Chowdhury, Saikat; Wigneshweraraj, Sivaramesh; Irschik, Herbert; Jansen, Rolf; Nixon, B Tracy; Knight, Jennifer; Weiss, Shimon; Ebright, Richard H
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.
Affiliation:
Howard Hughes Medical Institute, Waksman Institute, and Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ 08854, USA.
Citation:
Opening and closing of the bacterial RNA polymerase clamp. 2012, 337 (6094):591-5 Science
Journal:
Science (New York, N.Y.)
Issue Date:
3-Aug-2012
URI:
http://hdl.handle.net/10033/246442
DOI:
10.1126/science.1218716
PubMed ID:
22859489
Type:
Article
Language:
en
ISSN:
1095-9203
Appears in Collections:
Publications of RG Microbial Drugs (MWIS)

Full metadata record

DC FieldValue Language
dc.contributor.authorChakraborty, Anirbanen_GB
dc.contributor.authorWang, Dongyeen_GB
dc.contributor.authorEbright, Yon Wen_GB
dc.contributor.authorKorlann, Youen_GB
dc.contributor.authorKortkhonjia, Ekaterineen_GB
dc.contributor.authorKim, Taihoen_GB
dc.contributor.authorChowdhury, Saikaten_GB
dc.contributor.authorWigneshweraraj, Sivarameshen_GB
dc.contributor.authorIrschik, Herberten_GB
dc.contributor.authorJansen, Rolfen_GB
dc.contributor.authorNixon, B Tracyen_GB
dc.contributor.authorKnight, Jenniferen_GB
dc.contributor.authorWeiss, Shimonen_GB
dc.contributor.authorEbright, Richard Hen_GB
dc.date.accessioned2012-10-01T13:03:14Z-
dc.date.available2012-10-01T13:03:14Z-
dc.date.issued2012-08-03-
dc.identifier.citationOpening and closing of the bacterial RNA polymerase clamp. 2012, 337 (6094):591-5 Scienceen_GB
dc.identifier.issn1095-9203-
dc.identifier.pmid22859489-
dc.identifier.doi10.1126/science.1218716-
dc.identifier.urihttp://hdl.handle.net/10033/246442-
dc.description.abstractUsing 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.en_GB
dc.language.isoenen
dc.rightsArchived with thanks to Science (New York, N.Y.)en_GB
dc.subject.meshDNA Polymerase IIIen_GB
dc.subject.meshFluorescence Resonance Energy Transferen_GB
dc.subject.meshGene Expression Regulation, Bacterialen_GB
dc.subject.meshProtein Conformationen_GB
dc.subject.meshTranscription, Geneticen_GB
dc.titleOpening and closing of the bacterial RNA polymerase clamp.en
dc.typeArticleen
dc.contributor.departmentHoward Hughes Medical Institute, Waksman Institute, and Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ 08854, USA.en_GB
dc.identifier.journalScience (New York, N.Y.)en_GB

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