This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by An, F. Y.
Right arrow Articles by Clewell, D. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by An, F. Y.
Right arrow Articles by Clewell, D. B.

 Previous Article  |  Next Article 

Journal of Bacteriology, October 1999, p. 5915-5921, Vol. 181, No. 19
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Identification and Characterization of a Determinant (eep) on the Enterococcus faecalis Chromosome That Is Involved in Production of the Peptide Sex Pheromone cAD1

Florence Y. An,1 Mark C. Sulavik,2,dagger and Don B. Clewell1,3,*

Department of Biologic and Materials Sciences, School of Dentistry,1 and Department of Microbiology and Immunology,3 and Infectious Disease Unit,2 School of Medicine, The University of Michigan, Ann Arbor, Michigan 48109

Received 1 June 1999/Accepted 27 July 1999

Plasmid-free strains of Enterococcus faecalis secrete a peptide sex pheromone, cAD1, which specifically induces a mating response by donors carrying the hemolysin plasmid pAD1 or related elements. A determinant on the E. faecalis OG1X chromosome has been found to encode a 46.5-kDa protein that plays an important role in the production of the extracellular cAD1. Wild-type E. faecalis OG1X cells harboring a plasmid chimera carrying the determinant exhibited an eightfold enhanced production of cAD1, and plasmid-free cells carrying a mutated chromosomal determinant secreted undetectable or very low amounts of the pheromone. The production of other pheromones such as cPD1, cOB1, and cCF10 was also influenced, although there was no effect on the pheromone cAM373. The determinant, designated eep (for enhanced expression of pheromone), did not include the sequence of the pheromone. Its deduced product (Eep) contains apparent membrane-spanning sequences; conceivably it is involved in processing a pheromone precursor structure or in some way regulates expression or secretion.

* Corresponding author. Mailing address: Biologic and Materials Sciences, School of Dentistry, The University of Michigan, Ann Arbor, MI 48109-1078. Phone: (734) 763-0117. Fax: (734) 763-9905. E-mail: dclewell{at}umich.edu.

dagger Present address: Genome Therapeutics Corp., Waltham, MA 02154-8440.

Journal of Bacteriology, October 1999, p. 5915-5921, Vol. 181, No. 19
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Zhou, R., Cusumano, C., Sui, D., Garavito, R. M., Kroos, L. (2009). Intramembrane proteolytic cleavage of a membrane-tethered transcription factor by a metalloprotease depends on ATP. Proc. Natl. Acad. Sci. USA 106: 16174-16179 [Abstract] [Full Text]  
  • Denham, E. L., Ward, P. N., Leigh, J. A. (2008). Lipoprotein Signal Peptides Are Processed by Lsp and Eep of Streptococcus uberis. J. Bacteriol. 190: 4641-4647 [Abstract] [Full Text]  
  • Chandler, J. R., Dunny, G. M. (2008). Characterization of the Sequence Specificity Determinants Required for Processing and Control of Sex Pheromone by the Intramembrane Protease Eep and the Plasmid-Encoded Protein PrgY. J. Bacteriol. 190: 1172-1183 [Abstract] [Full Text]  
  • Dunny, G. M (2007). The peptide pheromone-inducible conjugation system of Enterococcus faecalis plasmid pCF10: cell-cell signalling, gene transfer, complexity and evolution. Phil Trans R Soc B 362: 1185-1193 [Abstract] [Full Text]  
  • Chandler, J. R., Hirt, H., Dunny, G. M. (2005). A paracrine peptide sex pheromone also acts as an autocrine signal to induce plasmid transfer and virulence factor expression in vivo. Proc. Natl. Acad. Sci. USA 102: 15617-15622 [Abstract] [Full Text]  
  • Visick, K. L., Fuqua, C. (2005). Decoding Microbial Chatter: Cell-Cell Communication in Bacteria. J. Bacteriol. 187: 5507-5519 [Full Text]  
  • Chandler, J. R., Flynn, A. R., Bryan, E. M., Dunny, G. M. (2005). Specific Control of Endogenous cCF10 Pheromone by a Conserved Domain of the pCF10-Encoded Regulatory Protein PrgY in Enterococcus faecalis. J. Bacteriol. 187: 4830-4843 [Abstract] [Full Text]  
  • Urban, S., Wolfe, M. S. (2005). Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity. Proc. Natl. Acad. Sci. USA 102: 1883-1888 [Abstract] [Full Text]  
  • Prince, H., Zhou, R., Kroos, L. (2005). Substrate Requirements for Regulated Intramembrane Proteolysis of Bacillus subtilis Pro-{sigma}K. J. Bacteriol. 187: 961-971 [Abstract] [Full Text]  
  • Friedmann, E., Lemberg, M. K., Weihofen, A., Dev, K. K., Dengler, U., Rovelli, G., Martoglio, B. (2004). Consensus Analysis of Signal Peptide Peptidase and Homologous Human Aspartic Proteases Reveals Opposite Topology of Catalytic Domains Compared with Presenilins. J. Biol. Chem. 279: 50790-50798 [Abstract] [Full Text]  
  • Bittencourt de Marques, E., Suzart, S. (2004). Occurrence of virulence-associated genes in clinical Enterococcus faecalis strains isolated in Londrina, Brazil. J Med Microbiol 53: 1069-1073 [Abstract] [Full Text]  
  • Zhang, L., Lin, J., Ji, G. (2004). Membrane Anchoring of the AgrD N-terminal Amphipathic Region Is Required for Its Processing to Produce a Quorum-sensing Pheromone in Staphylococcus aureus. J. Biol. Chem. 279: 19448-19456 [Abstract] [Full Text]  
  • Zhou, R., Kroos, L. (2004). BofA protein inhibits intramembrane proteolysis of pro-{sigma}K in an intercompartmental signaling pathway during Bacillus subtilis sporulation. Proc. Natl. Acad. Sci. USA 101: 6385-6390 [Abstract] [Full Text]  
  • Golde, T. E., Eckman, C. B. (2003). Physiologic and Pathologic Events Mediated by Intramembranous and Juxtamembranous Proteolysis. Sci Signal 2003: re4-re4 [Abstract] [Full Text]  
  • Gallio, M., Sturgill, G., Rather, P., Kylsten, P. (2002). A conserved mechanism for extracellular signaling in eukaryotes and prokaryotes. Proc. Natl. Acad. Sci. USA 99: 12208-12213 [Abstract] [Full Text]  
  • Alba, B. M., Leeds, J. A., Onufryk, C., Lu, C. Z., Gross, C. A. (2002). DegS and YaeL participate sequentially in the cleavage of RseA to activate the sigma E-dependent extracytoplasmic stress response. Genes Dev. 16: 2156-2168 [Abstract] [Full Text]  
  • An, F. Y., Clewell, D. B. (2002). Identification of the cAD1 Sex Pheromone Precursor in Enterococcus faecalis. J. Bacteriol. 184: 1880-1887 [Abstract] [Full Text]  
  • Antiporta, M. H., Dunny, G. M. (2002). ccfA, the Genetic Determinant for the cCF10 Peptide Pheromone in Enterococcus faecalis OG1RF. J. Bacteriol. 184: 1155-1162 [Abstract] [Full Text]  
  • Hirt, H., Schlievert, P. M., Dunny, G. M. (2002). In Vivo Induction of Virulence and Antibiotic Resistance Transfer in Enterococcus faecalis Mediated by the Sex Pheromone-Sensing System of pCF10. Infect. Immun. 70: 716-723 [Abstract] [Full Text]  
  • Buttaro, B. A. L., Antiporta, M. H., Dunny, G. M. (2000). Cell-Associated Pheromone Peptide (cCF10) Production and Pheromone Inhibition in Enterococcus faecalis. J. Bacteriol. 182: 4926-4933 [Abstract] [Full Text]  
  • Ye, J., Dave, U. P., Grishin, N. V., Goldstein, J. L., Brown, M. S. (2000). Asparagine-proline sequence within membrane-spanning segment of SREBP triggers intramembrane cleavage by Site-2 protease. Proc. Natl. Acad. Sci. USA 97: 5123-5128 [Abstract] [Full Text]  
  • Weihofen, A., Lemberg, M. K., Ploegh, H. L., Bogyo, M., Martoglio, B. (2000). Release of Signal Peptide Fragments into the Cytosol Requires Cleavage in the Transmembrane Region by a Protease Activity That Is Specifically Blocked by a Novel Cysteine Protease Inhibitor. J. Biol. Chem. 275: 30951-30956 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»