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Updated: Jul 10, 2026

An Assay for Quantifying Protein-RNA Binding in Bacteria
Published on: June 12, 2019
Mapping of RNA polymerase residues that interact with bacteriophage Xp10 transcription antitermination factor p7
Yulia Yuzenkova1, Nikolay Zenkin, Konstantin Severinov
1Waksman Institute for Microbiology Rutgers, The State University of New Jersey, Piscataway, NJ 08854, USA.
Abstract:
Bacteriophage Xp10-encoded transcription factor p7 interacts with host Xanthomonas oryzae RNA polymerase beta' subunit and prevents both promoter recognition by the RNA polymerase holoenzyme and transcription termination by the RNA polymerase core. P7 does not bind to and has no effect on RNA polymerase from Escherichia coli. Here, we use a combination of biochemical and genetic methods to map the p7 interaction site to within four beta' amino acid residues at the N terminus of X. oryzae RNAP beta'. The interaction site is located in an area that is close to the promoter spacer in the open complex and to the upstream boundary of the transcription bubble in the elongation complex, providing a possible explanation of how a small protein can affect both transcription initiation and termination by binding to the same RNA polymerase site.
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