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Papers In Press, published online ahead of print January 10, 2001
J. Biol. Chem, 10.1074/jbc.M009087200
Submitted on October 4, 2000
Revised on December 21, 2000
Accepted on January 10, 2001
Biochemistry and Molecular Biology, The Penn State University College of Medicine, Hershey, PA 17033
Corresponding Author: mfried{at}psu.edu
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.
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