Signaling Consequences of Structural Lesions that Alter the Stability of Chemoreceptor Trimers of Dimers.

ABSTRACT: Residues E402 and R404 of the Escherichia coli serine chemoreceptor, Tsr, appear to form a salt bridge that spans the interfaces between neighboring dimers in the Tsr trimer of dimers, a key structural component of receptor core signaling complexes. To assess their functional roles, we constructed full sets of single amino acid replacement mutants at E402 and R404 and characterized their signaling behaviors with a suite of in vivo assays. Our results indicate that the E402 and R404 residues of Tsr play their most critical signaling roles at their inner locations near the trimer axis where they likely participate in stabilizing the trimer-of-dimer packing and the kinase-ON state of core signaling complexes. Mutant receptors with a variety of side-chain replacements still accessed both the O

SUBMITTER: Lai RZ 

PROVIDER: S-EPMC5370551 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature