Youn Hwan, Carranza Marcus
Departments of Biology, California State University Fresno, Fresno, CA, 93740, USA.
J Microbiol. 2023 Mar;61(3):277-287. doi: 10.1007/s12275-023-00028-6. Epub 2023 Mar 9.
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.
将大肠杆菌环磷酸腺苷受体蛋白（CRP，一种典型的细菌转录因子）的活性和非活性结构进行比较，以建立环磷酸腺苷诱导的CRP激活范式。结果表明，所得范式与对CRP及CRP*（一组表现出无环磷酸腺苷活性的CRP突变体）的大量生化研究一致。CRP对环磷酸腺苷的亲和力由两个因素决定：（i）环磷酸腺苷口袋的有效性；（ii）脱辅基CRP的蛋白质平衡。讨论了这两个因素如何相互作用以决定CRP及CRP*突变体的环磷酸腺苷亲和力和环磷酸腺苷特异性。还描述了目前对CRP-DNA相互作用的理解以及知识空白。本综述最后列出了几个未来需要解决的重要CRP问题。
