Mass spectrometry and split luciferase complementation assays reveal the MecA protein interactome of Streptococcus mutans.

ABSTRACT: MecA is a highly conserved adaptor protein encoded by prokaryotes from the Bacillota phylum. MecA mutants exhibit similar pleiotropic defects in a variety of organisms, although most of these phenotypes currently lack a mechanistic basis. MecA mediates ClpCP-dependent proteolysis of its substrates, but only several such substrates have been reported in the literature and there are suggestions that proteolysis-independent regulatory mechanisms may also exist. Here, we provide the first comprehensive characterization of the MecA interactome and further assess its regulatory role in Clp-dependent proteolysis. Untargeted coimmunoprecipitation assays coupled with mass spectrometry revealed that the MecA ortholog from the oral pathobiont Streptococcus mutans likely serves as a majo

SUBMITTER: Qin H 

PROVIDER: S-EPMC10845952 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature