| Literature DB >> 16980448 |
Jiro Nakayama1, Shengmin Chen, Nozomi Oyama, Kenzo Nishiguchi, Essam A Azab, Emi Tanaka, Reiko Kariyama, Kenji Sonomoto.
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.Entities:
Mesh:
Substances:
Year: 2006 PMID: 16980448 PMCID: PMC1698201 DOI: 10.1128/JB.00865-06
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490