RT Journal Article
SR Electronic
T1 Septal Secretion of Protein A in <em>Staphylococcus aureus</em> Requires SecA and Lipoteichoic Acid Synthesis
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 245522
DO 10.1101/245522
A1 Wenqi Yu
A1 Dominique Missiakas
A1 Olaf Schneewind
YR 2018
UL http://biorxiv.org/content/early/2018/01/09/245522.abstract
AB Surface proteins of Staphylococcus aureus are secreted across septal membranes for assembly into the bacterial cross-wall. This localized secretion requires the YSIRK/GXXS motif signal peptide, however the mechanisms supporting precursor trafficking are not known. We show here that the signal peptide of staphylococcal protein A (SpA) is cleaved at the YSIRK/GXXS motif. A signal peptide mutant defective for cleavage can be crosslinked to SecA, SecDF and LtaS. SecA depletion blocks precursor targeting to septal membranes, whereas deletion of secDF diminishes SpA secretion into the cross-wall. Depletion of LtaS blocks lipoteichoic acid synthesis and promotes precursor trafficking to peripheral membranes. We propose a model whereby SecA directs SpA precursors to lipoteichoic acid-rich septal membranes for YSIRK/GXXS motif cleavage and secretion into the cross-wall.