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Changes in relative transcript amounts caused by ∆tprA, ∆phrA, double ∆tprA ∆phrA mutation or the addition of PhrA peptide in Streptococcus pneumoniae

ABSTRACT: Lantibiotics are highly modified peptides that are part of the bacteriocin family of antimicrobial peptides. We have identified a Phr peptide quorum sensing system (TprA/PhrA) that controls the expression of a lantibiotic gene cluster in the Gram-positive human pathogen, Streptococcus pneumoniae. We have characterized the basic mechanism for a Phr peptide signaling system in S. pneumoniae D39 and found that it induces expression of the lantibiotic genes when pneumococcal cells are at high density in the presence of galactose, a main sugar of the human nasopharynx, a highly competitive microbial environment. In this study we used RNA-seq analysis to examine the changes in relative transcript amounts caused by ∆tprA and ∆phrA mutations or the addition of the 10-residue synthetic PhrA peptide. These analyses reveal that PhrA peptide addition induces the transcription of a cluster of lantibiotic gene that appear to process and provide immunity to a lantibiotic peptide. In addition, TprA, a transcriptional factor regulated by a Phr peptide, autoregulates its own transcription.

ORGANISM(S): Streptococcus pneumoniae

PROVIDER: GSE68598 | GEO | 2015/10/20

SECONDARY ACCESSION(S): PRJNA283183

REPOSITORIES: GEO

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Project description:The induction of genetic competence is a strategy used by bacteria to increase their genetic repertoire under stressful environmental conditions. Recently, Streptococcus pneumoniae has been shown to co-ordinate the uptake of transforming DNA with fratricide via increased expression of the peptide pheromone responsible for competence induction. Here, we document that environmental stress-induced expression of the peptide pheromone competence-stimulating peptide (CSP) in the oral pathogen Streptococcus mutans. We showed that CSP is involved in the stress response and determined the CSP-induced regulon in S. mutans by microarray analysis. Contrary to pneumococcus, S. mutans responds to increased concentrations of CSP by cell lysis in only a fraction of the population. We have focused on the mechanism of cell lysis and have identified a novel bacteriocin as the M-bM-^@M-^Xdeath effectorM-bM-^@M-^Y. Most importantly, we showed that this bacteriocin causes cell death via a novel mechanism of action: intracellular action against self. We have also identified the cognate bacteriocin immunity protein, which resides in a separate unlinked genetic locus to allow its differential regulation. The role of the lytic response in S. mutans competence is also discussed. Together, these findings reveal a novel autolytic pathway in S. mutans which may be involved in the dissemination of fitness-enhancing genes in the oral biofilm. Streptococcus mutans UA159 were grown with 2 uM CSP or without (uninduced control) to mid-log phase. Total RNA was extracted as described above. The cDNAs were prepared for hybridization using the PFGRC protocol. Microarray chips were scanned using a Gene Pix 4000B (Axon) and analyzed using the TM4 Microarray Software Suite (http://www.tm4.org/). Transcript levels were measured by cDNA hybridized to a fourfold redundant S. mutans microarray and averaged for three replicated hybridizations. Differential gene expression was based on a post-normalization cut-off of M-BM-1> twofold.

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Changes in relative transcript amounts caused by ∆tprA, ∆phrA, double ∆tprA ∆phrA mutation or the addition of PhrA peptide in Streptococcus pneumoniae

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