Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1975 Jan;121(1):204–211. doi: 10.1128/jb.121.1.204-211.1975

Multiple mutations in cysA 14 MUTANTS OF Bacillus subtilis.

J F Kane, R L Goode, J Wainscott
PMCID: PMC285632  PMID: 803951

Abstract

Isolates of Bacillus subtilis that had been presumed to carry the cysA14 lesion have been studied. Our data indicate that these strains contain four mutations, all of which are linked by transformation and lie in the region of the ribosomal markers. The requirement for cysteine results from a defective serine transacetylase that is coded for by the cysA locus. Therefore, these mutants grow only in the presence of cysteine but not with sulfate, sulfite, or sulfide as the sole source of sulfur. A second genetic lesion (css) can be recognized by an increased sensitivity to the amino acid L-cysteine. The inhibited enzyme(s) has not been determined but inhibition is overcome by a mixture of eight amino acids. The third mutation (hts) results in the overproduction and excretion of hydrogen sulfide. This compound appears to be produced from cysteine by the enzyme cysteine desulfhydrylase and not by an increased activity of the sulfate-reductive pathway. This locus presumably codes for a regulatory element involved in the control of cysteine desulfhydrylase. The fourth mutation (cym) is not well characterized biochemically but results in a requirement for cysteine or methionine. The following order of these mutations has been established by transformation studies: hts, cysA, css, cym. The generally poor growth of these mutants in minimal-salts glucose media supplemented with cysteine can now be explained by these observations. The cysA14 mutants not only require an amino acid that is itself inhibitory to growth but they also overproduce the highly toxic compound hydrogen sulfide.

Full text

PDF
204

Images in this article

208Image
on p.208

Selected References

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

  1. Adiga P. R., Sarma P. S. Cysteine toxicity in Neurospora crassa: the mechanism of counteraction by amino acids. Indian J Biochem. 1971 Mar;8(1):9–15. [PubMed] [Google Scholar]
  2. Collins J. M., Wallenstein A., Monty K. J. Regulatory features of the cysteine desulfhydrase of Salmonella typhimurium. Biochim Biophys Acta. 1973 Jun 20;313(1):156–162. doi: 10.1016/0304-4165(73)90196-7. [DOI] [PubMed] [Google Scholar]
  3. DREYFUSS J., MONTY K. J. COINCIDENT REPRESSION OF THE REDUCTION OF 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE, SULFITE, AND THIOSULFATE IN THE CYSTEINE PATHWAY OF SALMONELLA TYPHIMURIUM. J Biol Chem. 1963 Nov;238:3781–3783. [PubMed] [Google Scholar]
  4. Dubnau D., Goldthwaite C., Smith I., Marmur J. Genetic mapping in Bacillus subtilis. J Mol Biol. 1967 Jul 14;27(1):163–185. doi: 10.1016/0022-2836(67)90358-0. [DOI] [PubMed] [Google Scholar]
  5. Goldthwaite C., Dubnau D., Smith I. Genetic mapping of antibiotic resistance in markers Bacillus subtilis. Proc Natl Acad Sci U S A. 1970 Jan;65(1):96–103. doi: 10.1073/pnas.65.1.96. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Harford N., Sueoka N. Chromosomal location of antibiotic resistance markers in Bacillus subtilis. J Mol Biol. 1970 Jul 28;51(2):267–286. doi: 10.1016/0022-2836(70)90142-7. [DOI] [PubMed] [Google Scholar]
  7. Haworth S. R., Brown L. R. Genetic analysis of ribonucleic acid polymerase mutants of Bacillus subtilis. J Bacteriol. 1973 Apr;114(1):103–113. doi: 10.1128/jb.114.1.103-113.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Jensen R. A. A biochemical basis for apparent abortive transformation in Bacillus subtilis. Genetics. 1968 Dec;60(4):707–717. doi: 10.1093/genetics/60.4.707. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Jones-Mortimer M. C., Wheldrake J. F., Pasternak C. A. The control of sulphate reduction in Escherichia coli by O-acetyl-L-serine. Biochem J. 1968 Mar;107(1):51–53. doi: 10.1042/bj1070051. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Kane J. F., Holmes W. M., Jensen R. A. Metabolic interlock. The dual function of a folate pathway gene as an extra-operonic gene of tryptophan biosynthesis. J Biol Chem. 1972 Mar 10;247(5):1587–1596. [PubMed] [Google Scholar]
  11. Kane J. F., Stenmark S. L., Calhoun D. H., Jensen R. A. Metabolic interlock. The role of the subordinate type of enzyme in the regulation of a complex pathway. J Biol Chem. 1971 Jul 10;246(13):4308–4316. [PubMed] [Google Scholar]
  12. Kari C., Nagy Z., Kovács P., Hernádi F. Mechanism of the growth inhibitory effect of cysteine on Escherichia coli. J Gen Microbiol. 1971 Nov;68(3):349–356. doi: 10.1099/00221287-68-3-349. [DOI] [PubMed] [Google Scholar]
  13. Kredich N. M., Tomkins G. M. The enzymic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium. J Biol Chem. 1966 Nov 10;241(21):4955–4965. [PubMed] [Google Scholar]
  14. Lobyreva L. B., Ruban E. L. Vliianie tsisteina na aktivnost' triptofansintetazy Candida utilis 295t. Mikrobiologiia. 1971 Jul-Aug;40(4):596–598. [PubMed] [Google Scholar]
  15. PASTERNAK C. A., ELLIS R. J., JONES-MORTIMER M. C., CRICHTON C. E. THE CONTROL OF SULPHATE REDUCTION IN BACTERIA. Biochem J. 1965 Jul;96:270–275. doi: 10.1042/bj0960270. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Piggot P. J. Mapping of asporogenous mutations of Bacillus subtilis: a minimum estimate of the number of sporeulation operons. J Bacteriol. 1973 Jun;114(3):1241–1253. doi: 10.1128/jb.114.3.1241-1253.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Smith D. A. S-amino acid metabolism and its regulation in Escherichia coli and Salmonella typhimurium. Adv Genet. 1971;16:141–165. doi: 10.1016/s0065-2660(08)60357-0. [DOI] [PubMed] [Google Scholar]
  18. Smith I., Smith H. Location of the SPO2 attachment site and the bryamycin resistance marker on the Bacillus subtilis chromosome. J Bacteriol. 1973 Jun;114(3):1138–1142. doi: 10.1128/jb.114.3.1138-1142.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES