Hide metadata

dc.date.accessioned2014-07-24T11:19:05Z
dc.date.available2014-07-24T11:19:05Z
dc.date.created2013-01-08T14:17:09Z
dc.date.issued2012
dc.identifier.citationKhan, Rabia Rukke, Håkon Valen Filho, Antonio Pedro Ricomini Fimland, Gunnar Arntzen, Magnus Thiede, Bernd Petersen, Fernanda Cristina . Extracellular Identification of a Processed Type II ComR/ComS Pheromone of Streptococcus mutans. Journal of Bacteriology. 2012, 194(15), 3781-3788
dc.identifier.urihttp://hdl.handle.net/10852/39400
dc.description.abstractThe competence-stimulating peptide (CSP) and the sigX-inducing peptide (XIP) are known to induce Streptococcus mutans competence for genetic transformation. For both pheromones, direct identification of the native peptides has not been accomplished. The fact that extracellular XIP activity was recently observed in a chemically defined medium devoid of peptides, as mentioned in an accompanying paper (K. Desai, L. Mashburn-Warren, M. J. Federle, and D. A. Morrison, J. Bacteriol. 194:3774–3780, 2012), provided ideal conditions for native XIP identification. To search for the XIP identity, culture supernatants were filtered to select for peptides of less than 3 kDa, followed by C18 extraction. One peptide, not detected in the supernatant of a comS deletion mutant, was identified by tandem mass spectrometry (MS/MS) fragmentation as identical to the ComS C-terminal sequence GLDWWSL. ComS processing did not require Eep, a peptidase involved in processing or import of bacterial small hydrophobic peptides, since eep deletion had no inhibitory effect on XIP production or on synthetic XIP response. We investigated whether extracellular CSP was also produced. A reporter assay for CSP activity detection, as well as MS analysis of supernatants, revealed that CSP was not present at detectable levels. In addition, a mutant with deletion of the CSP-encoding gene comC produced endogenous XIP levels similar to those of a nondeletion mutant. The results indicate that XIP pheromone production is a natural phenomenon that may occur in the absence of natural CSP pheromone activity and that the heptapeptide GLDWWSL is an extracellular processed form of ComS, possibly the active XIP pheromone. This is the first report of direct identification of a ComR/ComS pheromone.
dc.languageEN
dc.language.isoenen_US
dc.publisherAmerican Society for Microbiology
dc.titleExtracellular Identification of a Processed Type II ComR/ComS Pheromone of Streptococcus mutansen_US
dc.typeJournal articleen_US
dc.creator.authorKhan, Rabia
dc.creator.authorRukke, Håkon Valen
dc.creator.authorFilho, Antonio Pedro Ricomini
dc.creator.authorFimland, Gunnar
dc.creator.authorArntzen, Magnus
dc.creator.authorThiede, Bernd
dc.creator.authorPetersen, Fernanda Cristina
cristin.unitcode185,16,0,0
cristin.unitnameDet odontologiske fakultet
cristin.ispublishedtrue
cristin.fulltextoriginal
cristin.qualitycode2
dc.identifier.cristin983647
dc.identifier.bibliographiccitationinfo:ofi/fmt:kev:mtx:ctx&ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Journal of Bacteriology&rft.volume=194&rft.spage=3781&rft.date=2012
dc.identifier.jtitleJournal of Bacteriology
dc.identifier.volume194
dc.identifier.issue15
dc.identifier.startpage3781
dc.identifier.endpage3788
dc.identifier.doihttp://dx.doi.org/10.1128/JB.00624-12
dc.identifier.urnURN:NBN:no-44205
dc.type.documentTidsskriftartikkelen_US
dc.type.peerreviewedPeer reviewed
dc.source.issn0021-9193
dc.identifier.fulltextFulltext https://www.duo.uio.no/bitstream/handle/10852/39400/1/Extracellular+identification.pdf
dc.type.versionPublishedVersion


Files in this item

Appears in the following Collection

Hide metadata