Thioredoxin Profiling of Multiple Thioredoxin-Like Proteins in Staphylococcus aureus.

ABSTRACT: Hydrogen sulfide (H₂S) is thought to signal through protein S-sulfuration (persulfidation; S-sulfhydration) in both mammalian systems and bacteria. We previously profiled proteome S-sulfuration in Staphylococcus aureus (S. aureus) and identified two thioredoxin-like proteins, designated TrxP and TrxQ, that were capable of reducing protein persulfides as a potential regulatory mechanism. In this study, we further characterize TrxP, TrxQ and the canonical thioredoxin, TrxA, by identifying candidate protein substrates in S. aureus cells using a mechanism-based profiling assay where we trap mixed disulfides that exist between the attacking cysteine of a FLAG-tagged Trx and a persulfidated cysteine on the candidate substrate protein in cells.

SUBMITTER: Peng H 

PROVIDER: S-EPMC6196236 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature