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Originally published In Press as doi:10.1074/jbc.M009087200 on January 10, 2001

J. Biol. Chem., Vol. 276, Issue 14, 11226-11229, April 6, 2001
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In Vitro Interaction of the Escherichia coli Cyclic AMP Receptor Protein with the Lactose Repressor*

Michael G. FriedDagger and Margaret A. Daugherty§

From the Department of Biochemistry and Molecular Biology, Penn State University College of Medicine, Hershey, Pennsylvania 17033

Sedimentation equilibrium studies show that the Escherichia coli cyclic AMP receptor protein (CAP) and lactose repressor associate to form a 2:1 complex in vitro. This is, to our knowledge, the first demonstration of a direct interaction of these proteins in the absence of DNA. No 1:1 complex was detected over a wide range of CAP concentrations, suggesting that binding is highly cooperative. Complex formation is stimulated by cAMP, with a net uptake of 1 equivalent of cAMP per molecule of CAP bound. Substitution of the dimeric lacI-18 mutant repressor for tetrameric wild-type repressor completely eliminates detectable binding. We therefore propose that CAP binds the cleft between dimeric units in the repressor tetramer. CAP-lac repressor interactions may play important roles in regulatory events that take place at overlapping CAP and repressor binding sites in the lactose promoter.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 717-531-5250; Fax: 717-531-7072; E-mail: mfried@psu.edu.

§ Present address: Dept. of Biochemistry, Given B409, The University of Vermont College of Medicine, Burlington, VT 05405.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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