Signal peptidase SpsB coordinates staphylococcal cell cycle, surface protein septal trafficking and LTA synthesis.

ABSTRACT: Many cell wall anchored surface proteins of Gram-positive bacteria harbor a highly conserved YSIRK/G-S signal peptide (SP_YSIRK+), which deposits surface protein precursors at the cell division septum where they are subsequently anchored to septal peptidoglycan. Previously we identified that LtaS-mediated lipoteichoic acid (LTA) synthesis regulates septal trafficking of YSIRK+ proteins in S. aureus. Interestingly, both LtaS and SP_YSIRK+ are cleaved by the signal peptidase SpsB, but the biological implications remain unclear. Here we show that SpsB is required for cleaving SP_SpA(YSIRK+) of staphylococcal surface protein A (SpA). Depletion of spsB not only diminished SP_SpA processing but also abolished SpA septal localization. The mis-

SUBMITTER: Zhang R 

PROVIDER: S-EPMC11370438 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature