Allostery within a transcription coactivator is predominantly mediated through dissociation rate constants.

ABSTRACT: The kinase-inducible domain interacting (KIX) domain of CREB binding protein binds to multiple intrinsically disordered transcription factors in vivo at two distinct sites on its surface. Several reports have been made of allosteric communication between these two sites in this well-characterized model system. In this work, we have performed fluorescence stopped-flow measurements to investigate the kinetics of binding of five KIX binding proteins. We find that they all have similar association and dissociation rate constants for complex formation, despite their wide range of intrinsic helical propensities. Furthermore, by careful arrangement of pseudofirst-order conditions, we have been able to show that both association and dissociation rate constants are decreased when a partner is bound

SUBMITTER: Shammas SL 

PROVIDER: S-EPMC4143058 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature