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Gene Review

cysB  -  HTH-type transcriptional regulator CysB

Salmonella enterica subsp. enterica serovar Typhimurium str. LT2

 
 
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Disease relevance of cysB

 

High impact information on cysB

 

Biological context of cysB

  • The results do not support the concept of multiple cistrons at cysB and suggest that the abortive transductants previously observed in crosses between certain cysB mutants were due to intracistronic complementation [2].
  • Constitutive mutation of cysJIH operon in a cysB deletion strain of Salmonella typhimurium [6].
 

Associations of cysB with chemical compounds

  • The behavior of cysB mutants agrees with the hypothesis that, under some conditions, mecillinam action would be dependent on expression of the cysteine regulon [1].
  • We demonstrated that the cysB product functions in the regulation of the cysteine biosynthetic enzymes during both logarithmic growth and stationary phase [7].
  • O-Acetylserine sulfhydrylase B was depressed by growth on a poor sulfur source, and depression was dependent upon both a functional cysB regulatory gene product and the internal inducer of the cysteine biosynthetic pathway, O-acetyl-L-serine [8].
  • We treated three cysB mutants with chemical mutagens and selected 81 secondary mutants in which the inability to utilize sulfate was suppressed [7].
  • Fully derepressed levels of sulfite reductase and O-acetylserine sulfhydrylase in cysB plasmid-bearing strains were only 25% higher than in the wild type, suggesting that the product of this regulatory gene ordinarily is not a limiting factor in the expression of the cysteine regulon [9].
 

Other interactions of cysB

  • Leaky cysB mutants, which are sensitive to the beta-lactam antibiotic mecillinam, displayed partial induction, whereas mecillinam-resistant cysB and cysE mutants showed no induction [1].
  • Cysteine auxotrophs of Salmonella typhimurium mutated in cysB, cysI or cysJ grew with sulphate as a sulphur source when incubated under a hydrogen/carbon dioxide atmosphere [10].
  • The results suggest that mutations in cysB (regulation of the several cys operons) and also cysI and cysJ (sulphite reductase activity) can be circumvented during anaerobic growth under hydrogen [10].
 

Analytical, diagnostic and therapeutic context of cysB

References

  1. Induction of the cysteine regulon of Salmonella typhimurium in LB medium affects the response of cysB mutants to mecillinam. Antón, D.N. Curr. Microbiol. (2000) [Pubmed]
  2. Fine-structure genetic map of the cysB locus in Salmonella typhimurium. Cheney, R.W., Kredich, N.M. J. Bacteriol. (1975) [Pubmed]
  3. Hydroxyl radical footprints and half-site arrangements of binding sites for the CysB transcriptional activator of Salmonella typhimurium. Hryniewicz, M.M., Kredich, N.M. J. Bacteriol. (1995) [Pubmed]
  4. Involvement of cysB and cysE genes in the sensitivity of Salmonella typhimurium to mecillinam. Oppezzo, O.J., Antón, D.N. J. Bacteriol. (1995) [Pubmed]
  5. Negative autoregulation of cysB in Salmonella typhimurium: in vitro interactions of CysB protein with the cysB promoter. Ostrowski, J., Kredich, N.M. J. Bacteriol. (1991) [Pubmed]
  6. Constitutive mutation of cysJIH operon in a cysB deletion strain of Salmonella typhimurium. Ostrowski, J., Hulanicka, D. Mol. Gen. Genet. (1979) [Pubmed]
  7. Regulatory mutants and control of cysteine biosynthetic enzymes in Salmonella typhimurium. Borum, P.R., Monty, K.J. J. Bacteriol. (1976) [Pubmed]
  8. Regulation of O-acetylserine sulfhydrylase B by L-cysteine in Salmonella typhimurium. Hulanicka, M.D., Hallquist, S.G., Kredich, N.M., Mojica-A, T. J. Bacteriol. (1979) [Pubmed]
  9. Cloning and physical mapping of the cysB region of Salmonella typhimurium. Jagura-Burdzy, G., Kredich, N.M. J. Bacteriol. (1983) [Pubmed]
  10. Cysteine auxotrophs of Salmonella typhimurium which grow without cysteine in a hydrogen/carbon dioxide atmosphere. Barrett, E.L., Chang, G.W. J. Gen. Microbiol. (1979) [Pubmed]
  11. Identification of the Salmonella typhimurium cysB gene product by two-dimensional protein electrophoresis. Baptist, E.W., Hallquist, S.G., Kredich, N.M. J. Bacteriol. (1982) [Pubmed]
 
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