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Nucleic Acids Research, 1994, Vol. 22, No. 21 4375-4380
© 1994

MOLECULAR BIOLOGY

Interactions between the cyclic AMP receptor protein and the Alpha subunit of RNA polymerase at the Escherichia Coli galactose operon P1 Promoter

Adrian Attey1, Tamara Belyaeva, Nigel savery, Jim Hoggett1, Nobuyuki Fujita2, AKira Ishihama2 and Stephen Busby*

School of Biochemistry, University of Birmingham PO Box 363, Birmingham B15 2TT 1School of Biology, University of York York Yo1 5DD, UK 2National Institute of Genetics, Mishima Shizuoka-ken 411, Japan

*To whom correspondence should be addressed

Received August 8, 1994. Revised September 19, 1994. Accepted September 19, 1994.

DNAase I footprinting has been used to study open complexes between Escherichia coli RNA polymerase and the galactose operon P1 promoter, both in the absence and the presence of CRP (the cyclic AMP receptor protein, a transcription activator). From the effects of deletion of the C-terminal part of the RNA polymerase alpha subunit, we deduce that alpha binds at the upstream end of both the binary RNA polymerase – galP1 and ternary RNA polymerase – CRP – galP1 complexes. Disruption of the alpha-upstream contact suppresses open complex formation at galP1 at lower temperatures. In ternary RNA polymerase–CRP–galP1 complexes, alpha appears to make direct contact with Activating Region 1 in CRP. DNAase I footprinting has been used to detect and quantify interactions between purified alpha and CRP bound at galP1.


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