Molecular characterization of the Enterococcus faecalis cytolysin activator. 1991

R A Segarra, and M C Booth, and D A Morales, and M M Huycke, and M S Gilmore
Department of Microbiology and Immunology, University of Oklahoma College of Medicine, Oklahoma City 73190.

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.

UI MeSH Term Description Entries
D007109 Immunity Nonsusceptibility to the invasive or pathogenic effects of foreign microorganisms or to the toxic effect of antigenic substances. Immune Process,Immune Response,Immune Processes,Immune Responses,Process, Immune,Response, Immune
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001426 Bacterial Proteins Proteins found in any species of bacterium. Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial
D001483 Base Sequence The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA
D013293 Enterococcus faecalis A species of gram-positive, coccoid bacteria commonly isolated from clinical specimens and the human intestinal tract. Most strains are nonhemolytic. Streptococcus Group D,Streptococcus faecalis
D013381 Subtilisins A family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.- Alcalase,AprA-Subtilisin,Bacillus amyloliquefaciens Serine Protease,Bacillus subtilis Alkaline Proteinase,Carlsberg Subtilisin,Maxatase,Nagarse,Novo Alcalase,Profezim,Protease VII,Subtilisin 72,Subtilisin A,Subtilisin BPN',Subtilisin Carlsberg,Subtilisin DY,Subtilisin E,Subtilisin GX,Subtilisin Novo,Subtilopeptidase A,Alcalase, Novo,AprA Subtilisin,Subtilisin, Carlsberg
D029968 Escherichia coli Proteins Proteins obtained from ESCHERICHIA COLI. E coli Proteins

Related Publications

R A Segarra, and M C Booth, and D A Morales, and M M Huycke, and M S Gilmore
May 1999, Medical microbiology and immunology,
R A Segarra, and M C Booth, and D A Morales, and M M Huycke, and M S Gilmore
April 2013, Toxins,
R A Segarra, and M C Booth, and D A Morales, and M M Huycke, and M S Gilmore
February 1996, Antonie van Leeuwenhoek,
R A Segarra, and M C Booth, and D A Morales, and M M Huycke, and M S Gilmore
August 2014, Journal of chemotherapy (Florence, Italy),
R A Segarra, and M C Booth, and D A Morales, and M M Huycke, and M S Gilmore
December 2004, Science (New York, N.Y.),
R A Segarra, and M C Booth, and D A Morales, and M M Huycke, and M S Gilmore
January 2017, mSphere,
R A Segarra, and M C Booth, and D A Morales, and M M Huycke, and M S Gilmore
January 1995, Developments in biological standardization,
R A Segarra, and M C Booth, and D A Morales, and M M Huycke, and M S Gilmore
September 2004, The EMBO journal,
R A Segarra, and M C Booth, and D A Morales, and M M Huycke, and M S Gilmore
January 2002, Nature,
R A Segarra, and M C Booth, and D A Morales, and M M Huycke, and M S Gilmore
September 1996, Molecular microbiology,
Copied contents to your clipboard!