Rgg proteins associated with internalized small hydrophobic peptides: a new quorum‐sensing mechanism in streptococci

摘要: We identified a genetic context encoding transcriptional regulator of the Rgg family and small hydrophobic peptide (SHP) in nearly all streptococci suggested that it may be involved new quorumsensing mechanism, with SHP playing role pheromone. Here, we provide further support for this hypothesis by constructing phylogenetic tree Rgg-like proteins from Gram-positive bacteria studying shp/rgg1358 locus Streptococcus thermophilus LMD-9. shp1358 gene as target Rgg1358, used to confirm existence steps mechanism including secretion, maturation reimportation pheromone into cell. surface plasmon resonance demonstrate interaction between regulatory protein performed electrophoretic mobility shift assays assess binding promoter regions its genes. The active form was mass spectrometry. Our findings encodes two components novel quorum-sensing involving is detected reimported cell Ami oligopeptide transporter.