Journal
SCIENCE
Volume 337, Issue 6094, Pages 591-595Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1218716
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Funding
- NIH [GM037554, GM069937, GM069709, GM41376, AI072766]
- Howard Hughes Medical Institute Investigatorship
- BBSRC [BB/K000233/1, BB/E023703/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/E023703/1, BB/K000233/1] Funding Source: researchfish
- Direct For Biological Sciences [1244098] Funding Source: National Science Foundation
- Div Of Molecular and Cellular Bioscience [1244098] Funding Source: National Science Foundation
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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.
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