Open AccessPositioning of two alpha subunit carboxy-terminal domains of RNA polymerase at promoters by two transcription factors
Author(s) -
Katsuhiko Murakami,
Jeffrey T. Owens,
Tamara A. Belyaeva,
Claude F. Meares,
Stephen J. W. Busby,
Akira Ishihama
Publication year - 1997
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.94.21.11274
Subject(s) - rna polymerase , rna polymerase ii , microbiology and biotechnology , promoter , transcription factor ii d , transcription (linguistics) , protein subunit , polymerase , biology , specificity factor , rna polymerase ii holoenzyme , g alpha subunit , interleukin 10 receptor, alpha subunit , nuclease , rna , biochemistry , dna , gene , gene expression , linguistics , philosophy
Interactions between the cAMP receptor protein (CRP) and the carboxy-terminal regulatory domain (CTD) ofEscherichia 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.