Septal secretion of protein A in Staphylococcus aureus requires SecA and lipoteichoic acid synthesis

ELife
Wenqi YuOlaf Schneewind

Abstract

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 SpA signal peptide mutant defective for YSIRK/GXXS cleavage is also impaired for septal secretion and co-purifies with 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 abolishes SpA precursor trafficking to septal 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.

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Citations

Dec 1, 2018·Molecular & Cellular Proteomics : MCP·Konstantinos C TsolisAnastassios Economou
Mar 1, 2019·Molecular & Cellular Proteomics : MCP·Konstantinos C TsolisAnastassios Economou
Jul 4, 2019·Microbiology Spectrum·Olaf Schneewind, Dominique M Missiakas
Feb 10, 2019·Microbiology Spectrum·Olaf Schneewind, Dominique Missiakas
May 6, 2021·Molecular Microbiology·Ran ZhangWenqi Yu

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Methods Mentioned

BETA
fluorescence microscopy
immunoprecipitation
fluorescence microcopy
electron microscopy
PCR
X-ray
affinity purification

Software Mentioned

Image J
ExPASy
GraphPad Prism

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