Septal Secretion of Protein A in Staphylococcus aureus Requires Seca and Lipoteichoic Acid Synthesis
Document Type
Article
Publication Date
2018
Digital Object Identifier (DOI)
https://doi.org/10.7554/eLife.34092.001
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.
Rights Information
This work is licensed under a Creative Commons Attribution 4.0 License.
Was this content written or created while at USF?
No
Citation / Publisher Attribution
Microbiology and Infectious Disease, v. 7, art. e34092
Scholar Commons Citation
Yu, Wenqi; Missiakas, Dominique; and Schneewind, Olaf, "Septal Secretion of Protein A in Staphylococcus aureus Requires Seca and Lipoteichoic Acid Synthesis" (2018). Molecular Biosciences Faculty Publications. 118.
https://digitalcommons.usf.edu/bcm_facpub/118
