Skip to main content
NCBI home page
Applied and Environmental Microbiology logoLink to Applied and Environmental Microbiology
. 1994 Jan;60(1):45–50. doi: 10.1128/aem.60.1.45-50.1994

A bioassay based on recombinant DNA technology for determining selenium concentration.

M Reches 1, C Zhao 1, H Engelberg-Kulka 1
PMCID: PMC201267  PMID: 7509588

Abstract

The trace element selenium has recently attracted attention, particularly because (i) selenocysteine is involved in the active site of various prokaryotic and eukaryotic enzymes, some of which have a role in human health; (ii) selenocysteine incorporation into these proteins is coded by UGA codons; and (iii) as a result, selenocysteine is now considered to be the 21st amino acid in an expanded genetic code. Here, we built recombinant DNA constructs in which expression of the lac'Z gene is driven in Escherichia coli by UGA-directed selenocysteine incorporation. In this system, levels of beta-galactosidase activity are proportionally and specifically related to the presence and concentrations of several specific simple selenium derivatives. The system can thus be used as a sensitive bioassay for their determination. This bioassay is one of a few using recombinant DNA technology to provide a reporter for simple detection of a chemical trace element.

Full text

PDF
45

Images in this article

47Image
on p.47

Selected References

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

  1. Berry M. J., Banu L., Chen Y. Y., Mandel S. J., Kieffer J. D., Harney J. W., Larsen P. R. Recognition of UGA as a selenocysteine codon in type I deiodinase requires sequences in the 3' untranslated region. Nature. 1991 Sep 19;353(6341):273–276. doi: 10.1038/353273a0. [DOI] [PubMed] [Google Scholar]
  2. Berry M. J., Banu L., Larsen P. R. Type I iodothyronine deiodinase is a selenocysteine-containing enzyme. Nature. 1991 Jan 31;349(6308):438–440. doi: 10.1038/349438a0. [DOI] [PubMed] [Google Scholar]
  3. Böck A., Forchhammer K., Heider J., Baron C. Selenoprotein synthesis: an expansion of the genetic code. Trends Biochem Sci. 1991 Dec;16(12):463–467. doi: 10.1016/0968-0004(91)90180-4. [DOI] [PubMed] [Google Scholar]
  4. Casadaban M. J., Cohen S. N. Lactose genes fused to exogenous promoters in one step using a Mu-lac bacteriophage: in vivo probe for transcriptional control sequences. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4530–4533. doi: 10.1073/pnas.76.9.4530. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Chambers I., Frampton J., Goldfarb P., Affara N., McBain W., Harrison P. R. The structure of the mouse glutathione peroxidase gene: the selenocysteine in the active site is encoded by the 'termination' codon, TGA. EMBO J. 1986 Jun;5(6):1221–1227. doi: 10.1002/j.1460-2075.1986.tb04350.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Costilow R. N. Selenium requirement for the growth of Clostridium sporogenes with glycine as the oxidant in stickland reaction systems. J Bacteriol. 1977 Jul;131(1):366–368. doi: 10.1128/jb.131.1.366-368.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Curran J. F., Yarus M. Base substitutions in the tRNA anticodon arm do not degrade the accuracy of reading frame maintenance. Proc Natl Acad Sci U S A. 1986 Sep;83(17):6538–6542. doi: 10.1073/pnas.83.17.6538. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Dürre P., Andreesen J. R. Selenium-dependent growth and glycine fermentation by Clostridium purinolyticum. J Gen Microbiol. 1982 Jul;128(7):1457–1466. doi: 10.1099/00221287-128-7-1457. [DOI] [PubMed] [Google Scholar]
  9. Epp O., Ladenstein R., Wendel A. The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution. Eur J Biochem. 1983 Jun 1;133(1):51–69. doi: 10.1111/j.1432-1033.1983.tb07429.x. [DOI] [PubMed] [Google Scholar]
  10. Gray M. R., Colot H. V., Guarente L., Rosbash M. Open reading frame cloning: identification, cloning, and expression of open reading frame DNA. Proc Natl Acad Sci U S A. 1982 Nov;79(21):6598–6602. doi: 10.1073/pnas.79.21.6598. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Heider J., Baron C., Böck A. Coding from a distance: dissection of the mRNA determinants required for the incorporation of selenocysteine into protein. EMBO J. 1992 Oct;11(10):3759–3766. doi: 10.1002/j.1460-2075.1992.tb05461.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hill K. E., Lloyd R. S., Yang J. G., Read R., Burk R. F. The cDNA for rat selenoprotein P contains 10 TGA codons in the open reading frame. J Biol Chem. 1991 Jun 5;266(16):10050–10053. [PubMed] [Google Scholar]
  13. Ihnat M., Thomassen Y., Wolynetz M. S., Veillon C. Trace element data reliability in clinical chemistry-interlaboratory trials and reference materials. Acta Pharmacol Toxicol (Copenh) 1986;59 (Suppl 7):566–572. doi: 10.1111/j.1600-0773.1986.tb02827.x. [DOI] [PubMed] [Google Scholar]
  14. Kawakami K., Inada T., Nakamura Y. Conditionally lethal and recessive UGA-suppressor mutations in the prfB gene encoding peptide chain release factor 2 of Escherichia coli. J Bacteriol. 1988 Nov;170(11):5378–5381. doi: 10.1128/jb.170.11.5378-5381.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kopelowitz J., Hampe C., Goldman R., Reches M., Engelberg-Kulka H. Influence of codon context on UGA suppression and readthrough. J Mol Biol. 1992 May 20;225(2):261–269. doi: 10.1016/0022-2836(92)90920-f. [DOI] [PubMed] [Google Scholar]
  16. Mullenbach G. T., Tabrizi A., Irvine B. D., Bell G. I., Tainer J. A., Hallewell R. A. Selenocysteine's mechanism of incorporation and evolution revealed in cDNAs of three glutathione peroxidases. Protein Eng. 1988 Sep;2(3):239–246. doi: 10.1093/protein/2.3.239. [DOI] [PubMed] [Google Scholar]
  17. Nève J. Methods in determination of selenium states. J Trace Elem Electrolytes Health Dis. 1991 Mar;5(1):1–17. [PubMed] [Google Scholar]
  18. Nève J. Physiological and nutritional importance of selenium. Experientia. 1991 Feb 15;47(2):187–193. doi: 10.1007/BF01945424. [DOI] [PubMed] [Google Scholar]
  19. Read R., Bellew T., Yang J. G., Hill K. E., Palmer I. S., Burk R. F. Selenium and amino acid composition of selenoprotein P, the major selenoprotein in rat serum. J Biol Chem. 1990 Oct 15;265(29):17899–17905. [PubMed] [Google Scholar]
  20. Roesser J. R., Nakamura Y., Yanofsky C. Regulation of basal level expression of the tryptophan operon of Escherichia coli. J Biol Chem. 1989 Jul 25;264(21):12284–12288. [PubMed] [Google Scholar]
  21. Rotruck J. T., Pope A. L., Ganther H. E., Swanson A. B., Hafeman D. G., Hoekstra W. G. Selenium: biochemical role as a component of glutathione peroxidase. Science. 1973 Feb 9;179(4073):588–590. doi: 10.1126/science.179.4073.588. [DOI] [PubMed] [Google Scholar]
  22. Schoulaker-Schwarz R., Dekel-Gorodetsky L., Engelberg-Kulka H. An additional function for bacteriophage lambda rex: the rexB product prevents degradation of the lambda O protein. Proc Natl Acad Sci U S A. 1991 Jun 1;88(11):4996–5000. doi: 10.1073/pnas.88.11.4996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Stadtman T. C. Biosynthesis and function of selenocysteine-containing enzymes. J Biol Chem. 1991 Sep 5;266(25):16257–16260. [PubMed] [Google Scholar]
  24. Stadtman T. C. Selenium biochemistry. Annu Rev Biochem. 1990;59:111–127. doi: 10.1146/annurev.bi.59.070190.000551. [DOI] [PubMed] [Google Scholar]
  25. Sunde R. A. Molecular biology of selenoproteins. Annu Rev Nutr. 1990;10:451–474. doi: 10.1146/annurev.nu.10.070190.002315. [DOI] [PubMed] [Google Scholar]
  26. Yang G. Q., Chen J. S., Wen Z. M., Ge K. Y., Zhu L. Z., Chen X. C., Chen X. S. The role of selenium in Keshan disease. Adv Nutr Res. 1984;6:203–231. doi: 10.1007/978-1-4613-2801-8_8. [DOI] [PubMed] [Google Scholar]
  27. Zinoni F., Birkmann A., Leinfelder W., Böck A. Cotranslational insertion of selenocysteine into formate dehydrogenase from Escherichia coli directed by a UGA codon. Proc Natl Acad Sci U S A. 1987 May;84(10):3156–3160. doi: 10.1073/pnas.84.10.3156. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Zinoni F., Birkmann A., Stadtman T. C., Böck A. Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4650–4654. doi: 10.1073/pnas.83.13.4650. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Zinoni F., Heider J., Böck A. Features of the formate dehydrogenase mRNA necessary for decoding of the UGA codon as selenocysteine. Proc Natl Acad Sci U S A. 1990 Jun;87(12):4660–4664. doi: 10.1073/pnas.87.12.4660. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Applied and Environmental Microbiology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES