Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1990 Jan;172(1):473–476. doi: 10.1128/jb.172.1.473-476.1990

Intracellular serine protease 1 of Bacillus subtilis is formed in vivo as an unprocessed, active protease in stationary cells.

S M Sheehan 1, R L Switzer 1
PMCID: PMC208455  PMID: 2104610

Abstract

Western immunoblots and assays of Bacillus subtilis extracts showed that intracellular serine protease 1 is produced in a form larger than previously reported, appears not to have undergone N-terminal processing, and is active in the presence or absence of calcium. No evidence for an inactive precursor form of the protease was found.

Full text

PDF
473

Images in this article

474FIG. 1
on p.474

Selected References

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

  1. Band L., Henner D. J., Ruppen M. Construction and properties of an intracellular serine protease mutant of Bacillus subtilis. J Bacteriol. 1987 Jan;169(1):444–446. doi: 10.1128/jb.169.1.444-446.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Burnett T. J., Shankweiler G. W., Hageman J. H. Activation of intracellular serine proteinase in Bacillus subtilis cells during sporulation. J Bacteriol. 1986 Jan;165(1):139–145. doi: 10.1128/jb.165.1.139-145.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Burnette W. N. "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate--polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal Biochem. 1981 Apr;112(2):195–203. doi: 10.1016/0003-2697(81)90281-5. [DOI] [PubMed] [Google Scholar]
  4. Koide Y., Nakamura A., Uozumi T., Beppu T. Cloning and sequencing of the major intracellular serine protease gene of Bacillus subtilis. J Bacteriol. 1986 Jul;167(1):110–116. doi: 10.1128/jb.167.1.110-116.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Laemmli U. K., Favre M. Maturation of the head of bacteriophage T4. I. DNA packaging events. J Mol Biol. 1973 Nov 15;80(4):575–599. doi: 10.1016/0022-2836(73)90198-8. [DOI] [PubMed] [Google Scholar]
  6. Millet J. Characterization of a protein inhibitor of intracellular protease from Bacillus subtilis. FEBS Lett. 1977 Feb 15;74(1):59–61. doi: 10.1016/0014-5793(77)80752-7. [DOI] [PubMed] [Google Scholar]
  7. Millet J., Gregoire J. Characterization of an inhibitor of the intracellular protease from Bacillus subtilis. Biochimie. 1979;61(3):385–391. doi: 10.1016/s0300-9084(79)80132-7. [DOI] [PubMed] [Google Scholar]
  8. Neway J. O., Switzer R. L. Purification, characterization, and physiological function of Bacillus subtilis ornithine transcarbamylase. J Bacteriol. 1983 Aug;155(2):512–521. doi: 10.1128/jb.155.2.512-521.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Reysset G., Millet J. Characterization of an intracellular protease in B. subtillus during sporulation. Biochem Biophys Res Commun. 1972 Oct 17;49(2):328–334. doi: 10.1016/0006-291x(72)90414-7. [DOI] [PubMed] [Google Scholar]
  10. Ruppen M. E., Van Alstine G. L., Band L. Control of intracellular serine protease expression in Bacillus subtilis. J Bacteriol. 1988 Jan;170(1):136–140. doi: 10.1128/jb.170.1.136-140.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Schaeffer P., Millet J., Aubert J. P. Catabolic repression of bacterial sporulation. Proc Natl Acad Sci U S A. 1965 Sep;54(3):704–711. doi: 10.1073/pnas.54.3.704. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Srivastava O. P., Aronson A. I. Isolation and characterization of a unique protease from sporulating cells of Bacillus subtilis. Arch Microbiol. 1981 May;129(3):227–232. doi: 10.1007/BF00425256. [DOI] [PubMed] [Google Scholar]
  13. Stepanov V. M., Strongin A. Y., Izotova L. S., Abramov Z. T., Lyublinskaya L. A., Ermakova L. M., Baratova L. A., Belyanova L. P. Intracellular serine protease from Bacillus subtilis. Structural comparison with extracellular serine proteases-subtilisins. Biochem Biophys Res Commun. 1977 Jul 11;77(1):298–305. doi: 10.1016/s0006-291x(77)80196-4. [DOI] [PubMed] [Google Scholar]
  14. Strongin A. Y., Gorodetsky D. I., Kuznetsova I. A., Yanonis V. V., Abramov Z. T., Belyanova L. P., Baratova L. A., Stepanov V. M. Intracellular serine proteinase of Bacillus subtilis strain Marburg 168. Comparison with the homologous enzyme from Bacillus subtilis strain A-50. Biochem J. 1979 May 1;179(2):333–339. doi: 10.1042/bj1790333. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Strongin A. Y., Izotova L. S., Abramov Z. T., Ermakova L. M., Gorodetsky D. I., Stepanov V. M. On the appearance of Bacillus subtilis intracellular serine protease in the cell membrane and culture medium. Comparison of the enzyme and other Bacillus subtilis serine proteases. Arch Microbiol. 1978 Dec 20;119(3):287–293. doi: 10.1007/BF00405408. [DOI] [PubMed] [Google Scholar]
  16. Strongin A. Y., Izotova L. S., Abramov Z. T., Gorodetsky D. I., Ermakova L. M., Baratova L. A., Belyanova L. P., Stepanov V. M. Intracellular serine protease of Bacillus subtilis: sequence homology with extracellular subtilisins. J Bacteriol. 1978 Mar;133(3):1401–1411. doi: 10.1128/jb.133.3.1401-1411.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES