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dc.contributor.authorChakraborty, Anirban
dc.contributor.authorWang, Dongye
dc.contributor.authorEbright, Yon W
dc.contributor.authorKorlann, You
dc.contributor.authorKortkhonjia, Ekaterine
dc.contributor.authorKim, Taiho
dc.contributor.authorChowdhury, Saikat
dc.contributor.authorWigneshweraraj, Sivaramesh
dc.contributor.authorIrschik, Herbert
dc.contributor.authorJansen, Rolf
dc.contributor.authorNixon, B Tracy
dc.contributor.authorKnight, Jennifer
dc.contributor.authorWeiss, Shimon
dc.contributor.authorEbright, Richard H
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.
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
refterms.dateFOA2018-06-12T21:37:29Z
html.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.


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