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Minimal Machinery of RNA Polymerase Holoenzyme Sufficient for Promoter Melting
Brian A. Young,*Tanja M. Gruber,*Carol A. Gross
We determined the minimal portion of Escherichia coli RNA polymerase(RNAP) holoenzyme able to accomplish promoter melting, the crucialstep in transcription initiation that provides RNAP access tothe template strand. Upon duplex DNA binding, the N terminusof the ß' subunit (amino acids 1 to 314) and aminoacids 94 to 507 of the subunit, together comprising less thanone-fifth of RNAP holoenzyme, were able to melt an extended–10 promoter in a reaction remarkably similar to thatof authentic holoenzyme. Our results support the model thatcapture of nontemplate bases extruded from the DNA helix underliesthe melting process.
Departments of Stomatology and Microbiology and Immunology, University of California, San Francisco, San Francisco, CA 94143, USA.
* These authors contributed equally to the work.
To whom correspondence should be addressed. E-mail: cgross{at}cgl.ucsf.edu
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subunit, together comprising less than one-fifth of RNAP holoenzyme, were able to melt an extended –10 promoter in a reaction remarkably similar to that of authentic holoenzyme. Our results support the model that capture of nontemplate bases extruded from the DNA helix underlies the melting process. 
To whom correspondence should be addressed. E-mail: 
