Revised model for Enterococcus faecalis fsr quorum-sensing system: The small open reading frame fsrD encodes the gelatinase biosynthesis-activating pheromone propeptide corresponding to staphylococcal AgrD

Jiro Nakayama, Shengmin Chen, Nozomi Oyama, Kenzo Nishiguchi, Essam A. Azab, Emi Tanaka, Reiko Kariyama, Kenji Sonomoto

Research output: Contribution to journalArticle

68 Citations (Scopus)

Abstract

Gelatinase biosynthesis-activating pheromone (GBAP) is an autoinducing peptide involved in Enterococcus faecalis fsr quorum sensing, and its 11-amino-acid sequence has been identified in the C-terminal region of the 242-residue deduced fsrB product (J. Nakayama et al., Mol. Microbiol. 41:145-154, 2001). In this study, however, we demonstrated the existence of fsrD, encoding the GBAP propeptide, which is in frame with fsrB but is translated independently of fsrB. It was also demonstrated that FsrB′, an FsrD segment-truncated FsrB, functions as a cysteine protease-like processing enzyme to generate GBAP from FsrD. This revised model is consistent with the staphylococcal agr system.

Original languageEnglish
Pages (from-to)8321-8326
Number of pages6
JournalJournal of bacteriology
Volume188
Issue number23
DOIs
Publication statusPublished - Dec 2006

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology

Fingerprint Dive into the research topics of 'Revised model for Enterococcus faecalis fsr quorum-sensing system: The small open reading frame fsrD encodes the gelatinase biosynthesis-activating pheromone propeptide corresponding to staphylococcal AgrD'. Together they form a unique fingerprint.

  • Cite this