Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1986 Oct;168(1):322–327. doi: 10.1128/jb.168.1.322-327.1986

Cloning and characterization of the cysAMK region of Salmonella typhimurium.

M D Hulanicka, C Garrett, G Jagura-Burdzy, N M Kredich
PMCID: PMC213454  PMID: 3531173

Abstract

A total of 30 kilobases of DNA comprising the cysAMK region of S. typhimurium was cloned as a series of fragments in phage lambda 1059. The genetic organization of this region was established through studies of gene expression from fragments subcloned in pBR322 and from blot hydridization analyses of restriction sites in chromosomal DNA from multisite deletion strains. The results give a gene order of cysA-cysM-crr-ptsl-ptsH-cysK over a distance of approximately 12 kilobases. cysM and cysA have been cloned and expressed in pBR322; attempts to obtain stable pBR322 derivatives carrying cysK were unsuccessful.

Full text

PDF
324

Selected References

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

  1. Boronat A., Britton P., Jones-Mortimer M. C., Kornberg H. L., Lee L. G., Murfitt D., Parra F. Location on the Escherichia coli genome of a gene specifying O-acetylserine (thiol)-lyase. J Gen Microbiol. 1984 Mar;130(3):673–685. doi: 10.1099/00221287-130-3-673. [DOI] [PubMed] [Google Scholar]
  2. Britton P., Boronat A., Hartley D. A., Jones-Mortimer M. C., Kornberg H. L., Parra F. Phosphotransferase-mediated regulation of carbohydrate utilization in Escherichia coli K12: location of the gsr (tgs) and iex (crr) genes by specialized transduction. J Gen Microbiol. 1983 Feb;129(2):349–356. doi: 10.1099/00221287-129-2-349. [DOI] [PubMed] [Google Scholar]
  3. Cordaro J. C., Roseman S. Deletion mapping of the genes coding for HPr and enzyme I of the phosphoenolpyruvate: sugar phosphotransferase system in Salmonella typhimurium. J Bacteriol. 1972 Oct;112(1):17–29. doi: 10.1128/jb.112.1.17-29.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. DREYFUSS J. CHARACTERIZATION OF A SULFATE- AND THIOSULFATE-TRANSPORTING SYSTEM IN SALMONELLA TYPHIMURIUM. J Biol Chem. 1964 Jul;239:2292–2297. [PubMed] [Google Scholar]
  5. Gómez-Eichelmann M. C. Deoxyribonucleic acid adenine and cytosine methylation in Salmonella typhimurium and Salmonella typhi. J Bacteriol. 1979 Nov;140(2):574–579. doi: 10.1128/jb.140.2.574-579.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hartman P. E., Hartman Z., Stahl R. C. Classification and mapping of spontaneous and induced mutations in the histidine operon of Salmonella. Adv Genet. 1971;16:1–34. doi: 10.1016/s0065-2660(08)60352-1. [DOI] [PubMed] [Google Scholar]
  7. Hohn B. In vitro packaging of lambda and cosmid DNA. Methods Enzymol. 1979;68:299–309. doi: 10.1016/0076-6879(79)68021-7. [DOI] [PubMed] [Google Scholar]
  8. Holmes D. S., Quigley M. A rapid boiling method for the preparation of bacterial plasmids. Anal Biochem. 1981 Jun;114(1):193–197. doi: 10.1016/0003-2697(81)90473-5. [DOI] [PubMed] [Google Scholar]
  9. Hulanicka M. D., Hallquist S. G., Kredich N. M., Mojica-A T. Regulation of O-acetylserine sulfhydrylase B by L-cysteine in Salmonella typhimurium. J Bacteriol. 1979 Oct;140(1):141–146. doi: 10.1128/jb.140.1.141-146.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hulanicka M. D., Kredich N. M., Treiman D. M. The structural gene for O-acetylserine sulfhydrylase A in Salmonella typhimurium. Identity with the trzA locus. J Biol Chem. 1974 Feb 10;249(3):867–872. [PubMed] [Google Scholar]
  11. Inamine J. M., Burdett V. Structural organization of a 67-kilobase streptococcal conjugative element mediating multiple antibiotic resistance. J Bacteriol. 1985 Feb;161(2):620–626. doi: 10.1128/jb.161.2.620-626.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Jagura-Burdzy G., Kredich N. M. Cloning and physical mapping of the cysB region of Salmonella typhimurium. J Bacteriol. 1983 Aug;155(2):578–585. doi: 10.1128/jb.155.2.578-585.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Jones-Mortimer M. C. Positive control of sulphate reduction in Escherichia coli. The nature of the pleiotropic cysteineless mutants of E. coli K12. Biochem J. 1968 Dec;110(3):597–602. doi: 10.1042/bj1100597. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. 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]
  15. Karn J., Brenner S., Barnett L., Cesareni G. Novel bacteriophage lambda cloning vector. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5172–5176. doi: 10.1073/pnas.77.9.5172. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Kredich N. M. Regulation of L-cysteine biosynthesis in Salmonella typhimurium. I. Effects of growth of varying sulfur sources and O-acetyl-L-serine on gene expression. J Biol Chem. 1971 Jun 10;246(11):3474–3484. [PubMed] [Google Scholar]
  17. Lacks S., Greenberg B. Complementary specificity of restriction endonucleases of Diplococcus pneumoniae with respect to DNA methylation. J Mol Biol. 1977 Jul;114(1):153–168. doi: 10.1016/0022-2836(77)90289-3. [DOI] [PubMed] [Google Scholar]
  18. Maniatis T., Kee S. G., Efstratiadis A., Kafatos F. C. Amplification and characterization of a beta-globin gene synthesized in vitro. Cell. 1976 Jun;8(2):163–182. doi: 10.1016/0092-8674(76)90001-5. [DOI] [PubMed] [Google Scholar]
  19. Mayer H., Grosschedl R., Schütte H., Hobom G. ClaI. a new restriction endonuclease from Caryophanon latum L. Nucleic Acids Res. 1981 Oct 10;9(19):4833–4845. doi: 10.1093/nar/9.19.4833. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Meyers J. A., Sanchez D., Elwell L. P., Falkow S. Simple agarose gel electrophoretic method for the identification and characterization of plasmid deoxyribonucleic acid. J Bacteriol. 1976 Sep;127(3):1529–1537. doi: 10.1128/jb.127.3.1529-1537.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Mizobuchi K, Demerec M, Gillespie D H. Cysteine Mutants of Salmonella Typhimurium. Genetics. 1962 Nov;47(11):1617–1627. doi: 10.1093/genetics/47.11.1617. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Nakamura T., Iwahashi H., Eguchi Y. Enzymatic proof for the identity of the S-sulfocysteine synthase and cysteine synthase B of Salmonella typhimurium. J Bacteriol. 1984 Jun;158(3):1122–1127. doi: 10.1128/jb.158.3.1122-1127.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Nakamura T., Kon Y., Iwahashi H., Eguchi Y. Evidence that thiosulfate assimilation by Salmonella typhimurium is catalyzed by cysteine synthase B. J Bacteriol. 1983 Nov;156(2):656–662. doi: 10.1128/jb.156.2.656-662.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Sanderson K. E., Roth J. R. Linkage map of Salmonella typhimurium, Edition VI. Microbiol Rev. 1983 Sep;47(3):410–453. doi: 10.1128/mr.47.3.410-453.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Smith H. O., Birnstiel M. L. A simple method for DNA restriction site mapping. Nucleic Acids Res. 1976 Sep;3(9):2387–2398. doi: 10.1093/nar/3.9.2387. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Southern E. Gel electrophoresis of restriction fragments. Methods Enzymol. 1979;68:152–176. doi: 10.1016/0076-6879(79)68011-4. [DOI] [PubMed] [Google Scholar]
  27. Tu C. P., Cohen S. N. 3'-end labeling of DNA with [alpha-32P]cordycepin-5'-triphosphate. Gene. 1980 Jul;10(2):177–183. doi: 10.1016/0378-1119(80)90135-3. [DOI] [PubMed] [Google Scholar]
  28. VOGEL H. J., BONNER D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956 Jan;218(1):97–106. [PubMed] [Google Scholar]
  29. Yamamoto K. R., Alberts B. M., Benzinger R., Lawhorne L., Treiber G. Rapid bacteriophage sedimentation in the presence of polyethylene glycol and its application to large-scale virus purification. Virology. 1970 Mar;40(3):734–744. doi: 10.1016/0042-6822(70)90218-7. [DOI] [PubMed] [Google Scholar]
  30. Yang R., Lis J., Wu R. Elution of DNA from agarose gels after electrophoresis. Methods Enzymol. 1979;68:176–182. doi: 10.1016/0076-6879(79)68012-6. [DOI] [PubMed] [Google Scholar]

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

RESOURCES