This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Segarra, R A Articles by Gilmore, M S Search for Related Content PubMed PubMed Citation Articles by Segarra, R A Articles by Gilmore, M S

 Previous Article  |  Next Article 

Infect Immun. 1991 April; 59(4): 1239-1246

Molecular characterization of the Enterococcus faecalis cytolysin activator.

Department of Microbiology and Immunology, University of Oklahoma College of Medicine, Oklahoma City 73190.

ABSTRACT

The gene encoding component A (cylA), the activator protein of the Enterococcus faecalis cytolysin, has been localized on pAD1, and the nucleotide sequence was determined. cylA consists of a 1,236-bp open reading frame encoding a 412-amino-acid polypeptide. A search of the National Biomedical Research Foundation data base revealed significant homology between the inferred amino acid sequence of component A and subtilisin BPN'. Component A activation of the cytolysin precursor (component L) was observed to be inhibited by the serine protease inhibitor diisopropylfluorophosphate. Mature component A exhibits a molecular weight of approximately 30,000 and an isoelectric point of 4.5. Differences between the size of the primary translation product (45,625 daltons) and the mature enzyme suggest that, as for subtilisin, component A is secreted as a proenzyme. These results provide the basis for a model of component A activation of component L and a role for component A in protecting the cytolysin-producing cell from lysis.

This article has been cited by other articles:

• Tomita, H., Kamei, E., Ike, Y. (2008). Cloning and Genetic Analyses of the Bacteriocin 41 Determinant Encoded on the Enterococcus faecalis Pheromone-Responsive Conjugative Plasmid pYI14: a Novel Bacteriocin Complemented by Two Extracellular Components (Lysin and Activator). J. Bacteriol. 190: 2075-2085 [Abstract] [Full Text]  
• Coburn, P. S., Hancock, L. E., Booth, M. C., Gilmore, M. S. (1999). A Novel Means of Self-Protection, Unrelated to Toxin Activation, Confers Immunity to the Bactericidal Effects of the Enterococcus faecalis Cytolysin. Infect. Immun. 67: 3339-3347 [Abstract] [Full Text]