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KMID : 0880220230610030277
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Journal of Microbiology
2023 Volume.61 No. 3 p.277 ~ p.287
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cAMP Activation of the cAMP Receptor Protein, a Model Bacterial Transcription Factor
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Hwan Youn
Marcus Carranza
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Abstract
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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.
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KEYWORD
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CRP, cAMP affinity, cAMP specificity, CRP*, DNA binding
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