Positioning of two alpha subunit carboxy-terminal domains of RNA polymerase at promoters by two transcription factors.
Interactions between the cAMP receptor protein (CRP) and the carboxy-terminal regulatory domain (CTD) of Escherichia coli RNA polymerase alpha subunit were analyzed at promoters carrying tandem DNA sites for CRP binding using a chemical nuclease covalently attached to alpha. Each CRP dimer was found to direct the positioning of one of the two alpha subunit CTDs. Thus, the function of RNA polymerase may be subject to regulation through protein-protein interactions between the two alpha subunits and two different species of transcription factors.
Murakami
K
K
Department of Molecular Genetics, National Institute of Genetics, Mishima, Shizuoka 411, Japan.
Owens
J T
JT
Belyaeva
T A
TA
Meares
C F
CF
Busby
S J
SJ
Ishihama
A
A
D019943:Amino Acid Substitution; D001665:Binding Sites; D003545:Cysteine; D004247:DNA / Q000737:chemistry / Q000378:metabolism*; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry* / Q000378:metabolism*; D019281:Dimerization; D004926:Escherichia coli / Q000201:enzymology*; D015964:Gene Expression Regulation, Bacterial; D046911:Macromolecular Substances; D008961:Models, Structural; D016254:Mutagenesis, Insertional; D016297:Mutagenesis, Site-Directed; D016133:Polymerase Chain Reaction; D011401:Promoter Regions, Genetic; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D014157:Transcription Factors / Q000378:metabolism*; D014158:Transcription, Genetic
D046911:Macromolecular Substances; D011994:Recombinant Proteins; D014157:Transcription Factors; D004247:DNA; D012321:DNA-Directed RNA Polymerases; D003545:Cysteine