Asymmetric configurations in a reengineered homodimer reveal multiple subunit communication pathways in protein allostery.

ABSTRACT: Many allosteric proteins form homo-oligomeric complexes to regulate a biological function. In homo-oligomers, subunits establish communication pathways that are modulated by external stimuli like ligand binding. A challenge for dissecting the communication mechanisms in homo-oligomers is identifying intermediate liganded states, which are typically transiently populated. However, their identities provide the most mechanistic information on how ligand-induced signals propagate from bound to empty subunits. Here, we dissected the directionality and magnitude of subunit communication in a reengineered single-chain version of the homodimeric transcription factor cAMP receptor protein. By combining wild-type and mutant subunits in various asymmetric configurations, we revealed a linear relation

SUBMITTER: Lanfranco MF 

PROVIDER: S-EPMC5391741 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature