Title: | PptAB Exports Rgg Quorum-Sensing Peptides in Streptococcus |
Address: | "Department of Medicinal Chemistry and Pharmacognosy, Center for Biomolecular Sciences, College of Pharmacy, University of Illinois at Chicago, Chicago, Illinois, United States of America" |
DOI: | 10.1371/journal.pone.0168461 |
ISSN/ISBN: | 1932-6203 (Electronic) 1932-6203 (Linking) |
Abstract: | "A transposon mutagenesis screen designed to identify mutants that were defective in peptide-pheromone signaling of the Rgg2/Rgg3 pathway in Streptococcus pyogenes generated insertions in sixteen loci displaying diminished reporter activity. Fourteen unique transposon insertions were mapped to pptAB, an ABC-type transporter recently described to export sex pheromones of Enterococcus faecalis. Consistent with an idea that PptAB exports signaling peptides, the pheromones known as SHPs (short hydrophobic peptides) were no longer detected in cell-free culture supernatants in a generated deletion mutant of pptAB. PptAB exporters are conserved among the Firmicutes, but their function and substrates remain unclear. Therefore, we tested a pptAB mutant generated in Streptococcus mutans and found that while secretion of heterologously expressed SHP peptides required PptAB, secretion of the S. mutans endogenous pheromone XIP (sigX inducing peptide) was only partially disrupted, indicating that a secondary secretion pathway for XIP exists" |
Keywords: | "ATP-Binding Cassette Transporters/genetics/*metabolism Bacterial Proteins/genetics/*metabolism Bacterial Secretion Systems/*physiology DNA Transposable Elements Mutagenesis, Insertional Peptides/genetics/*metabolism Protein Transport/physiology Quorum Sen;" |
Notes: | "MedlineChang, Jennifer C Federle, Michael J eng R01 AI091779/AI/NIAID NIH HHS/ 2016/12/20 PLoS One. 2016 Dec 19; 11(12):e0168461. doi: 10.1371/journal.pone.0168461. eCollection 2016" |