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Opening and closing of the bacterial RNA polymerase clamp.

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.

SUBMITTER: Chakraborty A

PROVIDER: S-EPMC3626110 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature

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Opening and closing of the bacterial RNA polymerase clamp.

Chakraborty Anirban A Wang Dongye D Ebright Yon W YW Korlann You Y Kortkhonjia Ekaterine E Kim Taiho T Chowdhury Saikat S Wigneshweraraj Sivaramesh S Irschik Herbert H Jansen Rolf R Nixon B Tracy BT Knight Jennifer J Weiss Shimon S Ebright Richard H RH

Science (New York, N.Y.) 20120801 6094

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 inte ...[more]

PMID: 22859489

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