PMID:11152685

Citation	Fried, MG and Daugherty, MA (2001) In vitro interaction of the Escherichia coli cyclic AMP receptor protein with the lactose repressor. J. Biol. Chem. 276:11226-9
Abstract	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.
Links	PubMed Online version:10.1074/jbc.M009087200
Keywords	Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Cyclic AMP Receptor Protein/chemistry; Cyclic AMP Receptor Protein/metabolism; Escherichia coli/chemistry; Escherichia coli/metabolism; Escherichia coli Proteins; Lac Repressors; Protein Binding; Repressor Proteins/chemistry; Repressor Proteins/metabolism
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