Positioning of two alpha subunit carboxy-terminal domains of RNA polymerase at promoters by two transcription factors

Katsuhiko Murakami, Jeffrey T. Owens, Tamara A. Belyaeva, Claude F. Meares, Stephen J W Busby, Akira Ishihama

Research output: Contribution to journalArticle

75 Scopus citations


Interactions between the cAMP receptor protein (CRP) and the carboxy- terminal regulatory domain (CTD) of Escherichia coli RNA polymerase α subunit were analyzed at promoters carrying tandem DNA sites for CRP binding using a chemical nuclease covalently attached to α each CRP dimer was found to direct the positioning of one of the two α subunit CTDs. Thus, the function of RNA polymerase may be subject to regulation through protein- protein interactions between the two α subunits and two different species of transcription factors.

Original languageEnglish (US)
Pages (from-to)11274-11278
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number21
StatePublished - Oct 14 1997



  • Chemical nuclease
  • Protein-DNA contact
  • Protein-protein contact
  • Transcription regulation

ASJC Scopus subject areas

  • Genetics
  • General

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