| Title | cAMP Activation of the cAMP Receptor Protein, a Model Bacterial Transcription Factor |
|---|---|
| Author | Hwan Youn*, and Marcus Carranza |
| Address | Departments of Biology, California State University Fresno, Fresno, CA 93740, USA |
| Bibliography | Journal of Microbiology, 61(3),277-287, 2023, |
| DOI | 10.1007/s12275-023-00028-6 |
| Key Words | CRP · cAMP affinity · cAMP specificity · CRP* · DNA binding |
| 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. |