Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1978 Jun;134(3):1157–1170. doi: 10.1128/jb.134.3.1157-1170.1978

Properties of Bacillus cereus temperature-sensitive mutants altered in spore coat formation.

G N Stelma Jr, A I Aronson, P Fitz-James
PMCID: PMC222366  PMID: 96097

Abstract

Three conditional Bacillus cereus mutants altered in the assembly or formation of spore coat layers were analyzed. They all grew as well as the wild type in an enriched or minimal medium but produced lysozyme and octanol-sensitive spores at the nonpermissive temperature (35 to 38 degrees C). The spores also germinated slowly when produced at 35 degrees C. Temperature-shift experiments indicated that the defective protein or regulatory signal is expressed at the time of formation of the outer spore coat layers. Revertants regained all wild-type spore properties at frequencies consistent with initial point mutations. Spore coat defects were evident in thin sections and freeze-etch micrographs of mutant spores produced at 35 degrees C. In addition, one mutant contained an extra surface deposit, perhaps unprocessed spore coat precursor protein. A prevalent band of about 65,000 daltons (the same size as the presumptive precursor) was present in spore coat extracts of this mutant and may be incorrectly processed to mature spore coat polypeptides. Another class of mutants was defective in the late uptake of half-cystine residues into spore coats. Such a defect could lead to improper formation of the outer spore coat layers.

Full text

PDF
1159

Images in this article

1163Image
on p.1163
1165Image
on p.1165
1166Image
on p.1166
1167Image
on p.1167
1168Image
on p.1168

Selected References

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

  1. Aronson A. I., Angelo N., Holt S. C. Regulation of extracellular protease production in Bacillus cereus T: characterization of mutants producing altered amounts of protease. J Bacteriol. 1971 Jun;106(3):1016–1025. doi: 10.1128/jb.106.3.1016-1025.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Aronson A. I., Fitz-James P. C. Biosynthesis of bacterial spore coats. J Mol Biol. 1968 Apr 14;33(1):199–212. doi: 10.1016/0022-2836(68)90288-x. [DOI] [PubMed] [Google Scholar]
  3. Aronson A. I., Fitz-James P. C. Properties of Bacillus cereus spore coat mutants. J Bacteriol. 1975 Jul;123(1):354–365. doi: 10.1128/jb.123.1.354-365.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Aronson A. I., Fitz-James P. C. Reconstitution of bacterial spore coat layers in vitro. J Bacteriol. 1971 Oct;108(1):571–578. doi: 10.1128/jb.108.1.571-578.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Aronson A. I., Fitz-James P. Structure and morphogenesis of the bacterial spore coat. Bacteriol Rev. 1976 Jun;40(2):360–402. doi: 10.1128/br.40.2.360-402.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cheng Y. S., Aronson A. I. Alterations of spore coat processing and protein turnover in a Bacillus cereus mutant with a defective postexponential intracellular protease. Proc Natl Acad Sci U S A. 1977 Mar;74(3):1254–1258. doi: 10.1073/pnas.74.3.1254. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Fahey R. C., Brown W. C., Adams W. B., Worsham M. B. Occurrence of glutathione in bacteria. J Bacteriol. 1978 Mar;133(3):1126–1129. doi: 10.1128/jb.133.3.1126-1129.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Fairbanks G., Steck T. L., Wallach D. F. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 1971 Jun 22;10(13):2606–2617. doi: 10.1021/bi00789a030. [DOI] [PubMed] [Google Scholar]
  9. Fitz-James P. C. Formation of protoplasts from resting spores. J Bacteriol. 1971 Mar;105(3):1119–1136. doi: 10.1128/jb.105.3.1119-1136.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Horn D., Aronson A. I., Golub E. S. Development of a quantitative immunological assay for the study of spore coat synthesis and morphogenesis. J Bacteriol. 1973 Jan;113(1):313–321. doi: 10.1128/jb.113.1.313-321.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Ito J., Spizizen J. Increased rate of asporogenous mutations following treatment of Bacillus subtilis spores with ethyl methanesulfonate. Mutat Res. 1971 Sep;13(1):93–96. doi: 10.1016/0027-5107(71)90130-8. [DOI] [PubMed] [Google Scholar]
  12. JANSSEN F. W., LUND A. J., ANDERSON L. E. Colorimetric assay for dipicolinic acid in bacterial spores. Science. 1958 Jan 3;127(3288):26–27. doi: 10.1126/science.127.3288.26. [DOI] [PubMed] [Google Scholar]
  13. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  14. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  15. NAKATA H. M. ORGANIC NUTRIENTS REQUIRED FOR GROWTH AND SPORULATION OF BACILLUS CEREUS. J Bacteriol. 1964 Nov;88:1522–1524. doi: 10.1128/jb.88.5.1522-1524.1964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. NICKERSON W. J., DURAND S. C. KERATINASE. II. PROPERTIES OF THE CRYSTALLINE ENZYME. Biochim Biophys Acta. 1963 Sep 3;77:87–99. doi: 10.1016/0006-3002(63)90471-2. [DOI] [PubMed] [Google Scholar]
  17. NICKERSON W. J., NOVAL J. J., ROBISON R. S. KERATINASE. I. PROPERTIES OF THE ENZYME CONJUGATED ELABORATED BY STREPTOMYCES FRADIAE. Biochim Biophys Acta. 1963 Sep 3;77:73–86. doi: 10.1016/0006-3002(63)90470-0. [DOI] [PubMed] [Google Scholar]
  18. Vary J. C. Germination of Bacillus megaterium spores after various extraction procedures. J Bacteriol. 1973 Nov;116(2):797–802. doi: 10.1128/jb.116.2.797-802.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES