Organization of an activator-bound RNA polymerase holoenzyme

Molecular Cell
Daniel BoseXiaodong Zhang

Abstract

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.

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Citations

Nov 12, 2009·Proceedings of the National Academy of Sciences of the United States of America·Brian P HudsonCatherine L Lawson
May 5, 2010·Proceedings of the National Academy of Sciences of the United States of America·Patricia C BurrowsMartin Buck
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Methods Mentioned

BETA
NMR
footprinting
FRET
gel filtration
electron microscopy

Software Mentioned

Situs
CCP4
IMAGIC
EMAN
FindCTF2d

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