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TitleOrganization of an activator-bound RNA polymerase holoenzyme.
Journal, issue, pagesMol Cell, Vol. 32, Issue 3, Page 337-346, Year 2008
Publish dateNov 7, 2008
AuthorsDaniel Bose / Tillmann Pape / Patricia C Burrows / Mathieu Rappas / Siva R Wigneshweraraj / Martin Buck / Xiaodong Zhang /
PubMed AbstractTranscription initiation involves the conversion from closed promoter complexes, comprising RNA polymerase (RNAP) and double-stranded promoter DNA, to open complexes, in which the enzyme is able to ...Transcription initiation involves the conversion from closed promoter complexes, comprising RNA polymerase (RNAP) and double-stranded promoter DNA, to open complexes, in which the enzyme is able to access the DNA template in a single-stranded form. The complex between bacterial RNAP and its major variant sigma factor sigma(54) remains as a closed complex until ATP hydrolysis-dependent remodeling by activator proteins occurs. This remodeling facilitates DNA melting and allows the transition to the open complex. Here we present cryoelectron microscopy reconstructions of bacterial RNAP in complex with sigma(54) alone, and of RNAP-sigma(54) with an AAA+ activator. Together with photo-crosslinking data that establish the location of promoter DNA within the complexes, we explain why the RNAP-sigma(54) closed complex is unable to access the DNA template and propose how the structural changes induced by activator binding can initiate conformational changes that ultimately result in formation of the open complex.
External linksMol Cell / PubMed:18995832 / PubMed Central
MethodsEM (single particle)
Resolution21.0 - 23.0 Å
Structure data

EMDB-1566:
Activator bound RNA polymerase holoenzyme
Method: EM (single particle) / Resolution: 21.0 Å

EMDB-1567:
Sigma 54 RNA polymerase holoenzyme
Method: EM (single particle) / Resolution: 21.0 Å

EMDB-1568:
E.coli core RNA polymerase
Method: EM (single particle) / Resolution: 23.0 Å

Source
  • Escherichia coli (E. coli)
  • Klebsiella pneumoniae (bacteria)

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