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. 1970 Jun;66(2):480–487. doi: 10.1073/pnas.66.2.480

Cyclic AMP Receptor Protein of E. coli: Its Role in the Synthesis of Inducible Enzymes

Michael Emmer 1,2,*, Benoit deCrombrugghe 1,2,†, Ira Pastan 1,2,†, Robert Perlman 1,2,*
PMCID: PMC283070  PMID: 4317918

Abstract

A cyclic AMP binding protein has been purified over 100-fold from E. coli extracts. Protein purified from wild-type strains binds cyclic AMP with an apparent dissociation constant of 1-2 × 10-6 M. Two mutant strains that are unresponsive to exogenous cyclic AMP have altered binding activity; the protein purified from one of these mutants has a decreased affinity for cyclic AMP (apparent dissociation constant = 2 × 10-5 M). Extracts of this mutant are deficient in their ability to support β-galactosidase synthesis in vitro. The addition of purified, wild-type binding protein to these extracts restores enzyme synthesis toward normal. Because this binding protein appears to be required for cyclic AMP action, we suggest it be called the cyclic AMP receptor protein (CR protein).

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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