Revised Model for <i>Enterococcus faecalis fsr</i> Quorum-Sensing System: the Small Open Reading Frame <i>fsrD</i> 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

Journal of Bacteriology · 2006 · 116 citations · 21 references

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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.

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