Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1992 Mar;174(6):1844–1847. doi: 10.1128/jb.174.6.1844-1847.1992

In vivo processing of Staphylococcus aureus lipase.

J Rollof 1, S Normark 1
PMCID: PMC205786  PMID: 1548232

Abstract

The Staphylococcus aureus lipase gene encodes a 76-kDa protein. Extracellular lipase purified from culture supernatants is only 45 to 46 kDa, however. We show that the lipase is secreted in vivo as an 82-kDa protein with full enzymatic activity. It is then sequentially processed, both in culture and in cell-free supernatants, to a mature, 45- to 46-kDa protein. Protein sequencing demonstrates that the N-terminal region of the 82-kDa prolipase, comprising 295 amino acids, is cleaved from the central and C-terminal moieties, which contain the active site. A metallocysteine protease is probably responsible for initiating this processing. The extremely hydrophobic, mature lipase is resistant to further protease degradation and retains the full catalytic activity of the prolipase.

Full text

PDF
1845

Images in this article

1845Image
on p.1845
1846Image
on p.1846

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Buttke T. M., Cuchens M. A. Inhibition of lymphocyte proliferation by free fatty acids. II. Toxicity of stearic acid towards phytohaemagglutinin-activated T cells. Immunology. 1984 Nov;53(3):507–514. [PMC free article] [PubMed] [Google Scholar]
  2. Eftimiadi C., Buzzi E., Tonetti M., Buffa P., Buffa D., van Steenbergen M. T., de Graaff J., Botta G. A. Short-chain fatty acids produced by anaerobic bacteria alter the physiological responses of human neutrophils to chemotactic peptide. J Infect. 1987 Jan;14(1):43–53. doi: 10.1016/s0163-4453(87)90808-5. [DOI] [PubMed] [Google Scholar]
  3. Götz F., Popp F., Korn E., Schleifer K. H. Complete nucleotide sequence of the lipase gene from Staphylococcus hyicus cloned in Staphylococcus carnosus. Nucleic Acids Res. 1985 Aug 26;13(16):5895–5906. doi: 10.1093/nar/13.16.5895. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Hawley H. P., Gordon G. B. The effects of long chain free fatty acids on human neutrophil function and structure. Lab Invest. 1976 Feb;34(2):216–222. [PubMed] [Google Scholar]
  5. Hedström S. A. Lipolytic activity of Staphylococcus aureus strains from cases of human chronic osteomyelitis and other infections. Acta Pathol Microbiol Scand B. 1975 Jun;83(3):285–292. doi: 10.1111/j.1699-0463.1975.tb00102.x. [DOI] [PubMed] [Google Scholar]
  6. Klauser T., Pohlner J., Meyer T. F. Extracellular transport of cholera toxin B subunit using Neisseria IgA protease beta-domain: conformation-dependent outer membrane translocation. EMBO J. 1990 Jun;9(6):1991–1999. doi: 10.1002/j.1460-2075.1990.tb08327.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Kugimiya W., Otani Y., Hashimoto Y., Takagi Y. Molecular cloning and nucleotide sequence of the lipase gene from Pseudomonas fragi. Biochem Biophys Res Commun. 1986 Nov 26;141(1):185–190. doi: 10.1016/s0006-291x(86)80352-7. [DOI] [PubMed] [Google Scholar]
  8. Kyte J., Doolittle R. F. A simple method for displaying the hydropathic character of a protein. J Mol Biol. 1982 May 5;157(1):105–132. doi: 10.1016/0022-2836(82)90515-0. [DOI] [PubMed] [Google Scholar]
  9. Lee C. Y., Iandolo J. J. Lysogenic conversion of staphylococcal lipase is caused by insertion of the bacteriophage L54a genome into the lipase structural gene. J Bacteriol. 1986 May;166(2):385–391. doi: 10.1128/jb.166.2.385-391.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Lee C. Y., Iandolo J. J. Mechanism of bacteriophage conversion of lipase activity in Staphylococcus aureus. J Bacteriol. 1985 Oct;164(1):288–293. doi: 10.1128/jb.164.1.288-293.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Lowe M. E., Rosenblum J. L., Strauss A. W. Cloning and characterization of human pancreatic lipase cDNA. J Biol Chem. 1989 Nov 25;264(33):20042–20048. [PubMed] [Google Scholar]
  12. Rollof J., Braconier J. H., Söderström C., Nilsson-Ehle P. Interference of Staphylococcus aureus lipase with human granulocyte function. Eur J Clin Microbiol Infect Dis. 1988 Aug;7(4):505–510. doi: 10.1007/BF01962601. [DOI] [PubMed] [Google Scholar]
  13. Rollof J., Hedström S. A., Nilsson-Ehle P. Lipolytic activity of Staphylococcus aureus strains from disseminated and localized infections. Acta Pathol Microbiol Immunol Scand B. 1987 Apr;95(2):109–113. doi: 10.1111/j.1699-0463.1987.tb03096.x. [DOI] [PubMed] [Google Scholar]
  14. Rollof J., Hedström S. A., Nilsson-Ehle P. Purification and characterization of a lipase from Staphylococcus aureus. Biochim Biophys Acta. 1987 Sep 25;921(2):364–369. doi: 10.1016/0005-2760(87)90038-5. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES