cAMP Activation of the cAMP Receptor Protein, a Model Bacterial Transcription Factor

Hwan Youn; Marcus Carranza

doi:10.1007/s12275-023-00028-6

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cAMP Activation of the cAMP Receptor Protein, a Model Bacterial Transcription Factor: Hwan Youn , Marcus Carranza; Journal of Microbiology 2023;61(3):277-287.
DOI: https://doi.org/10.1007/s12275-023-00028-6
Published online: March 9, 2023

Departments of Biology, California State University Fresno, Fresno, CA 93740, USA

Corresponding author: Hwan Youn ,

Received: 27 December 2022 • Revised: 9 February 2023 • Accepted: 13 February 2023

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Abstract

The active and inactive structures of the Escherichia coli cAMP receptor protein (CRP), a model bacterial transcr!ption factor, are compared to generate a paradigm in the cAMP-induced activation of CRP. The resulting paradigm is shown to be consistent with numerous biochemical studies of CRP and CRP*, a group of CRP mutants displaying cAMP-free activity. The cAMP affinity of CRP is dictated by two factors: (i) the effectiveness of the cAMP pocket and (ii) the protein equilibrium of apo-CRP. How these two factors interplay in determining the cAMP affinity and cAMP specificity of CRP and CRP* mutants are discussed. Both the current understanding and knowledge gaps of CRP-DNA interactions are also described. This review ends with a list of several important CRP issues that need to be addressed in the future.

Keywords: CRP · cAMP affinity · cAMP specificity · CRP* · DNA binding

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cAMP Activation of the cAMP Receptor Protein, a Model Bacterial Transcription Factor

J. Microbiol. 2023;61(3):277-287. Published online March 9, 2023

DOI: https://doi.org/10.1007/s12275-023-00028-6

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