Kinetic partitioning between alternative protein-protein interactions controls a transcriptional switch.

ABSTRACT: Proteins can perform completely distinct functions in response to the particular partners that they bind to. Consequently, determination of the mechanism of functional regulation in such systems requires elucidation of the mechanism switching between binding partners. The central protein of the Escherichia coli biotin regulatory system, BirA, switches between its function as a metabolic enzyme or a transcriptional repressor in response to binding either the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase or a second BirA monomer. These two protein-protein interactions are structurally mutually exclusive. The results of earlier studies suggest that the system is regulated by kinetic partitioning between the two protein-protein interactions. In this work, sedimentation velo

SUBMITTER: Zhao H 

PROVIDER: S-EPMC2566847 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature