Affiliation:
1. Departments of Stomatology and Microbiology and Immunology, University of California, San Francisco, San Francisco, CA 94143, USA.
Abstract
We determined the minimal portion of
Escherichia coli
RNA polymerase (RNAP) holoenzyme able to accomplish promoter melting, the crucial step in transcription initiation that provides RNAP access to the template strand. Upon duplex DNA binding, the N terminus of the β′ subunit (amino acids 1 to 314) and amino acids 94 to 507 of the σ 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.
Publisher
American Association for the Advancement of Science (AAAS)
Reference23 articles.
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3. Protein−Nucleic Acid Interactions during Open Complex Formation Investigated by Systematic Alteration of the Protein and DNA Binding Partners
4. RNA Polymerase II/TFIIF Structure and Conserved Organization of the Initiation Complex
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Cited by
71 articles.
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