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. 1975 Feb;121(2):406–410. doi: 10.1128/jb.121.2.406-410.1975

Production and possible function of serine protease during sporulation of Bacillus subtilis.

B N Dancer, J Mandelstam
PMCID: PMC245944  PMID: 803477

Abstract

The production of extracellular protease during sporulation in Bacillus subtilis 168 was investigated. Two proteases are produced, an alkaline serine protease and a neutral metalloprotease. In vivo inhibition of the serine protease with phenylmethylsulfonylfluoride indicated that the metalloprotease was degraded by the serine protease during sporulation. The experiments with phenylmethylsulfonylfluoride also show that the serine protease is necessary for the sequential process of sporulation and that it is required continuously for the first 2 to 3 h of the 8-h process.

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Selected References

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

  1. Coote J. G., Mandelstam J. Use of constructed double mutants for determining the temporal order of expression of sporulation genes in Bacillus subtilis. J Bacteriol. 1973 Jun;114(3):1254–1263. doi: 10.1128/jb.114.3.1254-1263.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Coote J. G., Wood D. A., Mandelstam J. Lethal effect of rifampicin in Bacillus subtilis as a complicating factor in the assessment of the lifetime of messenger ribonucleic acid. Biochem J. 1973 May;134(1):263–270. doi: 10.1042/bj1340263. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Dancer B. N., Mandelstam J. Criteria for categorizing early biochemical events occurring during sporulation of Bacillus subtilis. J Bacteriol. 1975 Feb;121(2):411–415. doi: 10.1128/jb.121.2.411-415.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. GUNTELBERG A. V., OTTESEN M. Purification of the proteolytic enzyme from Bacillus subtilis. C R Trav Lab Carlsberg Chim. 1954;29(3-4):36–48. [PubMed] [Google Scholar]
  5. Goldberg A. L. Effects of protease inhibitors on protein breakdown and enzyme induction in starving Escherichia coli. Nat New Biol. 1971 Nov 10;234(45):51–52. doi: 10.1038/newbio234051a0. [DOI] [PubMed] [Google Scholar]
  6. Hageman J. H., Carlton B. C. Effects of mutational loss of specific intracellular proteases on the sporulation of Bacillus subtilis. J Bacteriol. 1973 May;114(2):612–617. doi: 10.1128/jb.114.2.612-617.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. MCCONN J. D., TSURU D., YASUNOBU K. T. BACILLUS SUBTILIS NEUTRAL PROTEINASE. I. A ZINC ENZYME OF HIGH SPECIFIC ACTIVITY. J Biol Chem. 1964 Nov;239:3706–3715. [PubMed] [Google Scholar]
  8. Mandelstam J., Waites W. M. Sporulation in Bacillus subtilis. The role of exoprotease. Biochem J. 1968 Oct;109(5):793–801. doi: 10.1042/bj1090793. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Michel J. F., Millet J. Physiological studies on early-blocked sporulation mutants of Bacillus subtilis. J Appl Bacteriol. 1970 Mar;33(1):220–227. doi: 10.1111/j.1365-2672.1970.tb05246.x. [DOI] [PubMed] [Google Scholar]
  10. Millet J. Caractérisation de deux endopeptidases excrétées par B. subtilis Marburg au cours de la sporulation. Bull Soc Chim Biol (Paris) 1969 Jul 25;51(3):457–469. [PubMed] [Google Scholar]
  11. Millet J. Characterization of proteinases excreted by Bacillus subtilis Marburg strain during sporulation. J Appl Bacteriol. 1970 Mar;33(1):207–219. doi: 10.1111/j.1365-2672.1970.tb05245.x. [DOI] [PubMed] [Google Scholar]
  12. Prestidge L., Gage V., Spizizen J. Protease activities during the course of sporulation on Bacillus subtilis. J Bacteriol. 1971 Sep;107(3):815–823. doi: 10.1128/jb.107.3.815-823.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Prouty W. F., Goldberg A. L. Effects of protease inhibitors on protein breakdown in Escherichia coli. J Biol Chem. 1972 May 25;247(10):3341–3352. [PubMed] [Google Scholar]
  14. Rinderknecht H., Geokas M. C., Silverman P., Haverback B. J. A new ultrasensitive method for the determination of proteolytic activity. Clin Chim Acta. 1968 Aug;21(2):197–203. doi: 10.1016/0009-8981(68)90127-7. [DOI] [PubMed] [Google Scholar]
  15. Ryter A., Schaeffer P., Ionesco H. Classification cytologique, par leur stade de blocage, des mutants de sporulation de Bacillus subtilis Marburg. Ann Inst Pasteur (Paris) 1966 Mar;110(3):305–315. [PubMed] [Google Scholar]
  16. Schaeffer P. Sporulation and the production of antibiotics, exoenzymes, and exotonins. Bacteriol Rev. 1969 Mar;33(1):48–71. doi: 10.1128/br.33.1.48-71.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Sterlini J. M., Mandelstam J. Commitment to sporulation in Bacillus subtilis and its relationship to development of actinomycin resistance. Biochem J. 1969 Jun;113(1):29–37. doi: 10.1042/bj1130029. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. TORRIANI A. Influence of inorganic phosphate in the formation of phosphatases by Escherichia coli. Biochim Biophys Acta. 1960 Mar 11;38:460–469. doi: 10.1016/0006-3002(60)91281-6. [DOI] [PubMed] [Google Scholar]
  19. Waites W. M., Kay D., Dawes I. W., Wood D. A., Warren S. C., Mandelstam J. Sporulation in Bacillus subtilis. Correlation of biochemical events with morphological changes in asporogenous mutants. Biochem J. 1970 Jul;118(4):667–676. doi: 10.1042/bj1180667. [DOI] [PMC free article] [PubMed] [Google Scholar]

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