Overproduction of the cyclic AMP receptor protein of Escherichia coli and expression of the engineered C-terminal DNA-binding domain

Biochem J. 1986 Jun 15;236(3):643-9. doi: 10.1042/bj2360643.


Overproduction of the cyclic AMP receptor protein (CRP) from Escherichia coli, up to 25% of the soluble cell protein, has been achieved in an inducible host-vector system under transcriptional control of the lambda promoter PL. This system is ideally suited for large scale production and purification of CRP. In addition, a structural gene for the DNA-binding domain of CRP has been constructed. To this end the nucleotide sequence coding for the C-terminus was fused to the sequence coding for the first 10 N-terminal amino acids and cloned into suitable vectors. Good expression was achieved using the lambda PL promoter. The gene product, beta CRP, is recognized by anti-CRP antibodies.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • DNA, Bacterial / genetics*
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / genetics*
  • Gene Expression Regulation
  • Genetic Engineering
  • Immunoelectrophoresis
  • Plasmids
  • Receptors, Cyclic AMP / biosynthesis
  • Receptors, Cyclic AMP / genetics*
  • Transformation, Genetic


  • DNA, Bacterial
  • Receptors, Cyclic AMP