CAMP is an allosteric modulator of DNA-binding specificity in the cAMP receptor protein from Mycobacterium tuberculosis.

ABSTRACT: Allosteric proteins with multiple subunits and ligand-binding sites are central in regulating biological signals. The cAMP receptor protein from Mycobacterium tuberculosis (CRP_MTB) is a global regulator of transcription composed of two identical subunits, each one harboring structurally conserved cAMP- and DNA-binding sites. The mechanisms by which these four binding sites are allosterically coupled in CRP_MTB remain unclear. Here, we investigate the binding mechanism between CRP_MTB and cAMP, and the linkage between cAMP and DNA interactions. Using calorimetric and fluorescence-based assays, we find that cAMP binding is entropically driven and displays negative cooperativity. Fluorescence anisotropy experiments show that apo-CRP_MTB forms high-orde

SUBMITTER: Garate F 

PROVIDER: S-EPMC8026907 | biostudies-literature | 2021 Jan-Jun

REPOSITORIES: biostudies-literature