cAMP-CRP activator complex and the CytR repressor protein bind co-operatively 
to the cytRP promoter in Escherichia coli and CytR antagonizes the 
cAMP-CRP-induced DNA bend

Pedersen, H.; Sogaard-Andersen, Lotte; Holst, B.; Gerlach, P.; Bremer, E.; Valentin-Hansen, P.

doi:10.1016/0022-2836(92)90896-R

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cAMP-CRP activator complex and the CytR repressor protein bind co-operatively to the cytRP promoter in Escherichia coli and CytR antagonizes the cAMP-CRP-induced DNA bend

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Citation

Pedersen, H., Sogaard-Andersen, L., Holst, B., Gerlach, P., Bremer, E., & Valentin-Hansen, P. (1992). cAMP-CRP activator complex and the CytR repressor protein bind co-operatively to the cytRP promoter in Escherichia coli and CytR antagonizes the cAMP-CRP-induced DNA bend. JOURNAL OF MOLECULAR BIOLOGY, 227(2), 396-406. doi:10.1016/0022-2836(92)90896-R.

Cite as: https://hdl.handle.net/21.11116/0000-0008-D681-4

Abstract

Initiation of transcription from the cytRP promoter in Escherichia coli is activated by the cAMP-CRP complex and negatively regulated by the CytR repressor protein. By combining gel retardation and footprinting assays, we show that cAMP-CRP binds to a single site centered at position -64 and induces a considerable bend in the DNA. CytR binds to a region immediately downstream from, and partially overlapping, the CRP site, and induces a modest bend into the DNA. In combination, cAMP-CRP and CytR bind co-operatively to cytRP forming a nucleoprotein complex in which the proteins directly interact with each other and bind to the same face of the DNA helix. CytR binding concomitantly antagonizes the cAMP-CRP-induced bend. This study indicates that the minimal DNA region required to obtain CytR regulation consists of a single binding site for each of cAMP-CRP and CytR. The case described here, in which a protein-induced DNA bend is modulated by a second protein, may illustrate a mechanism that applies to other regulatory systems.