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

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Abstract

The active and inactive structures of the Escherichia coli cAMP receptor protein (CRP), a model bacterial transcription 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.

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Acknowledgements

This work was supported by National Institutes of Health Grant R15AI101919 from the NIAID (to H. Y.). The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.

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

    Hwan Youn & Marcus Carranza

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Youn, H., Carranza, M. cAMP Activation of the cAMP Receptor Protein, a Model Bacterial Transcription Factor. J Microbiol. 61, 277–287 (2023). https://doi.org/10.1007/s12275-023-00028-6

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