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. 1995 Jul;177(14):4134–4136. doi: 10.1128/jb.177.14.4134-4136.1995

Sulfate and thiosulfate transport in Escherichia coli K-12: evidence for a functional overlapping of sulfate- and thiosulfate-binding proteins.

A Sirko 1, M Zatyka 1, E Sadowy 1, D Hulanicka 1
PMCID: PMC177147  PMID: 7608089

Abstract

In Escherichia coli, sulfate and thiosulfate ions are transported by an ABC-type transporter consisting of both the membrane components (the products of cysT, cysW, and cysA genes) and the periplasmic binders (the products of cysP and sbp genes). The single cysP and sbp mutants are able to utilize both sulfate and thiosulfate as a sole sulfur source, while the inactivation of both genes leads to cysteine auxotrophy resulting from the block in the transport of both ions.

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Selected References

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  1. Adams M. D., Oxender D. L. Bacterial periplasmic binding protein tertiary structures. J Biol Chem. 1989 Sep 25;264(27):15739–15742. [PubMed] [Google Scholar]
  2. Ames G. F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu Rev Biochem. 1986;55:397–425. doi: 10.1146/annurev.bi.55.070186.002145. [DOI] [PubMed] [Google Scholar]
  3. Ames G. F., Mimura C. S., Holbrook S. R., Shyamala V. Traffic ATPases: a superfamily of transport proteins operating from Escherichia coli to humans. Adv Enzymol Relat Areas Mol Biol. 1992;65:1–47. doi: 10.1002/9780470123119.ch1. [DOI] [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. Dreyfuss J., Pardee A. B. Evidence for a sulfate-binding site external to the cell membrane of Salmonella typhimurium. Biochim Biophys Acta. 1965 Jun 15;104(1):308–310. doi: 10.1016/0304-4165(65)90256-4. [DOI] [PubMed] [Google Scholar]
  6. Hellinga H. W., Evans P. R. Nucleotide sequence and high-level expression of the major Escherichia coli phosphofructokinase. Eur J Biochem. 1985 Jun 3;149(2):363–373. doi: 10.1111/j.1432-1033.1985.tb08934.x. [DOI] [PubMed] [Google Scholar]
  7. Hryniewicz M. M., Kredich N. M. The cysP promoter of Salmonella typhimurium: characterization of two binding sites for CysB protein, studies of in vivo transcription initiation, and demonstration of the anti-inducer effects of thiosulfate. J Bacteriol. 1991 Sep;173(18):5876–5886. doi: 10.1128/jb.173.18.5876-5886.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hryniewicz M., Sirko A., Hulanicka D. Identification and mapping of the sulphate permease promoter region in Escherichia coli. Acta Biochim Pol. 1989;36(3-4):353–363. [PubMed] [Google Scholar]
  9. Hryniewicz M., Sirko A., Pałucha A., Böck A., Hulanicka D. Sulfate and thiosulfate transport in Escherichia coli K-12: identification of a gene encoding a novel protein involved in thiosulfate binding. J Bacteriol. 1990 Jun;172(6):3358–3366. doi: 10.1128/jb.172.6.3358-3366.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hulanicka D., Klopotowski T., Smith D. A. The effect of triazole on cysteine biosynthesis in Salmonella typhimurium. J Gen Microbiol. 1972 Sep;72(2):291–301. doi: 10.1099/00221287-72-2-291. [DOI] [PubMed] [Google Scholar]
  11. Jacobson B. L., He J. J., Vermersch P. S., Lemon D. D., Quiocho F. A. Engineered interdomain disulfide in the periplasmic receptor for sulfate transport reduces flexibility. Site-directed mutagenesis and ligand-binding studies. J Biol Chem. 1991 Mar 15;266(8):5220–5225. [PubMed] [Google Scholar]
  12. Kohara Y., Akiyama K., Isono K. The physical map of the whole E. coli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library. Cell. 1987 Jul 31;50(3):495–508. doi: 10.1016/0092-8674(87)90503-4. [DOI] [PubMed] [Google Scholar]
  13. Kredich N. M. The molecular basis for positive regulation of cys promoters in Salmonella typhimurium and Escherichia coli. Mol Microbiol. 1992 Oct;6(19):2747–2753. doi: 10.1111/j.1365-2958.1992.tb01453.x. [DOI] [PubMed] [Google Scholar]
  14. Nikaido K., Ames G. F. Purification and characterization of the periplasmic lysine-, arginine-, ornithine-binding protein (LAO) from Salmonella typhimurium. J Biol Chem. 1992 Oct 15;267(29):20706–20712. [PubMed] [Google Scholar]
  15. Ota N., Galsworthy P. R., Pardee A. B. Genetics of sulfate transport by Salmonella typhimurium. J Bacteriol. 1971 Mar;105(3):1053–1062. doi: 10.1128/jb.105.3.1053-1062.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Pardee A. B., Prestidge L. S., Whipple M. B., Dreyfuss J. A binding site for sulfate and its relation to sulfate transport into Salmonella typhimurium. J Biol Chem. 1966 Sep 10;241(17):3962–3969. [PubMed] [Google Scholar]
  17. Pflugrath J. W., Quiocho F. A. The 2 A resolution structure of the sulfate-binding protein involved in active transport in Salmonella typhimurium. J Mol Biol. 1988 Mar 5;200(1):163–180. doi: 10.1016/0022-2836(88)90341-5. [DOI] [PubMed] [Google Scholar]
  18. Rao N. N., Torriani A. Molecular aspects of phosphate transport in Escherichia coli. Mol Microbiol. 1990 Jul;4(7):1083–1090. doi: 10.1111/j.1365-2958.1990.tb00682.x. [DOI] [PubMed] [Google Scholar]
  19. Sirko A., Hryniewicz M., Hulanicka D., Böck A. Sulfate and thiosulfate transport in Escherichia coli K-12: nucleotide sequence and expression of the cysTWAM gene cluster. J Bacteriol. 1990 Jun;172(6):3351–3357. doi: 10.1128/jb.172.6.3351-3357.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Speiser D. M., Ames G. F. Salmonella typhimurium histidine periplasmic permease mutations that allow transport in the absence of histidine-binding proteins. J Bacteriol. 1991 Feb;173(4):1444–1451. doi: 10.1128/jb.173.4.1444-1451.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Tam R., Saier M. H., Jr Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol Rev. 1993 Jun;57(2):320–346. doi: 10.1128/mr.57.2.320-346.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Winans S. C., Elledge S. J., Krueger J. H., Walker G. C. Site-directed insertion and deletion mutagenesis with cloned fragments in Escherichia coli. J Bacteriol. 1985 Mar;161(3):1219–1221. doi: 10.1128/jb.161.3.1219-1221.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]

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