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. 1986 Dec;83(24):9393–9397. doi: 10.1073/pnas.83.24.9393

Structural analysis of a rat liver glutathione S-transferase Ya gene.

C A Telakowski-Hopkins, G S Rothkopf, C B Pickett
PMCID: PMC387144  PMID: 3025841

Abstract

We have isolated and characterized a complete structural gene encoding a rat liver glutathione S-transferase (glutathione transferase; EC 2.5.1.18) Ya subunit. The gene spans approximately 11 kilobases and is comprised of seven exons separated by six introns. A sequence similar to the Goldberg-Hogness promoter ("TATA" box), TATTA, is located 32 base pairs upstream from the transcription initiation site. Exons 2 and 4 of the glutathione S-transferase gene encode amino acid sequences of the Ya subunit that are highly conserved in the Yc subunit, whereas exons 3 and 5 encode amino acids that are divergent in the Yc subunit. These data suggest that exons 2 and 4 may encode domains of the Ya subunits that have similar structural or functional properties to the corresponding domains in the Yc subunit (e.g., glutathione binding site), whereas exons 3 and 5 may encode domains of the Ya subunit that have unique structural or functional properties to the corresponding domains in the Yc subunit (e.g., substrate binding site).

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Selected References

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

  1. Bass N. M., Kirsch R. E., Tuff S. A., Marks I., Saunders S. J. Ligandin heterogeneity : evidence that the two non-identical subunits are the monomers of two distinct proteins. Biochim Biophys Acta. 1977 May 27;492(1):163–175. doi: 10.1016/0005-2795(77)90223-9. [DOI] [PubMed] [Google Scholar]
  2. Beale D., Ketterer B., Carne T., Meyer D., Taylor J. B. Evidence that the Ya and Yc subunits of glutathione transferase B (ligandin) are the products of separate genes. Eur J Biochem. 1982 Sep 1;126(3):459–463. doi: 10.1111/j.1432-1033.1982.tb06802.x. [DOI] [PubMed] [Google Scholar]
  3. Boyer T. D., Kenney W. C., Zakim D. Structural, functional and hybridization studies of the glutathione S-transferases of rat liver. Biochem Pharmacol. 1983 Jun 15;32(12):1843–1850. doi: 10.1016/0006-2952(83)90048-5. [DOI] [PubMed] [Google Scholar]
  4. Breathnach R., Chambon P. Organization and expression of eucaryotic split genes coding for proteins. Annu Rev Biochem. 1981;50:349–383. doi: 10.1146/annurev.bi.50.070181.002025. [DOI] [PubMed] [Google Scholar]
  5. Daniel V., Sarid S., Bar-Nun S., Litwack G. Rat ligandin mRNA molecular cloning and sequencing. Arch Biochem Biophys. 1983 Nov;227(1):266–271. doi: 10.1016/0003-9861(83)90370-3. [DOI] [PubMed] [Google Scholar]
  6. Ding G. J., Ding V. D., Rodkey J. A., Bennett C. D., Lu A. Y., Pickett C. B. Rat liver glutathione S-transferases. DNA sequence analysis of a Yb2 cDNA clone and regulation of the Yb1 and Yb2 mRNAs by phenobarbital. J Biol Chem. 1986 Jun 15;261(17):7952–7957. [PubMed] [Google Scholar]
  7. Ding G. J., Lu A. Y., Pickett C. B. Rat liver glutathione S-transferases. Nucleotide sequence analysis of a Yb1 cDNA clone and prediction of the complete amino acid sequence of the Yb1 subunit. J Biol Chem. 1985 Oct 25;260(24):13268–13271. [PubMed] [Google Scholar]
  8. Ding V. D., Pickett C. B. Transcriptional regulation of rat liver glutathione S-transferase genes by phenobarbital and 3-methylcholanthrene. Arch Biochem Biophys. 1985 Aug 1;240(2):553–559. doi: 10.1016/0003-9861(85)90062-1. [DOI] [PubMed] [Google Scholar]
  9. Gubler U., Hoffman B. J. A simple and very efficient method for generating cDNA libraries. Gene. 1983 Nov;25(2-3):263–269. doi: 10.1016/0378-1119(83)90230-5. [DOI] [PubMed] [Google Scholar]
  10. Hayes J. D. Purification and characterization of glutathione S-transferases P, S and N. Isolation from rat liver of Yb1 Yn protein, the existence of which was predicted by subunit hybridization in vitro. Biochem J. 1984 Dec 15;224(3):839–852. doi: 10.1042/bj2240839. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kalinyak J. E., Taylor J. M. Rat glutathione S-transferase. Cloning of double-stranded cDNA and induction of its mRNA. J Biol Chem. 1982 Jan 10;257(1):523–530. [PubMed] [Google Scholar]
  12. Ketterer B., Beale D., Taylor J. B., Meyer D. J. The genetic relationships and inducibility of soluble glutathione transferases of the rat liver. Biochem Soc Trans. 1983 Aug;11(4):466–467. doi: 10.1042/bst0110466. [DOI] [PubMed] [Google Scholar]
  13. Litwack G., Ketterer B., Arias I. M. Ligandin: a hepatic protein which binds steroids, bilirubin, carcinogens and a number of exogenous organic anions. Nature. 1971 Dec 24;234(5330):466–467. doi: 10.1038/234466a0. [DOI] [PubMed] [Google Scholar]
  14. Mannervik B. The isoenzymes of glutathione transferase. Adv Enzymol Relat Areas Mol Biol. 1985;57:357–417. doi: 10.1002/9780470123034.ch5. [DOI] [PubMed] [Google Scholar]
  15. Peacock S. L., McIver C. M., Monahan J. J. Transformation of E. coli using homopolymer-linked plasmid chimeras. Biochim Biophys Acta. 1981 Sep 28;655(2):243–250. doi: 10.1016/0005-2787(81)90014-9. [DOI] [PubMed] [Google Scholar]
  16. Pickett C. B., Telakowski-Hopkins C. A., Ding G. J., Argenbright L., Lu A. Y. Rat liver glutathione S-transferases. Complete nucleotide sequence of a glutathione S-transferase mRNA and the regulation of the Ya, Yb, and Yc mRNAs by 3-methylcholanthrene and phenobarbital. J Biol Chem. 1984 Apr 25;259(8):5182–5188. [PubMed] [Google Scholar]
  17. Reddy C. C., Li N., Tu C. P. Identification of a new glutathione S-transferase from rat liver cytosol. Biochem Biophys Res Commun. 1984 Jun 29;121(3):1014–1020. doi: 10.1016/0006-291x(84)90778-2. [DOI] [PubMed] [Google Scholar]
  18. Rothkopf G. S., Telakowski-Hopkins C. A., Stotish R. L., Pickett C. B. Multiplicity of glutathione S-transferase genes in the rat and association with a type 2 Alu repetitive element. Biochemistry. 1986 Mar 11;25(5):993–1002. doi: 10.1021/bi00353a007. [DOI] [PubMed] [Google Scholar]
  19. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Satoh K., Kitahara A., Soma Y., Inaba Y., Hatayama I., Sato K. Purification, induction, and distribution of placental glutathione transferase: a new marker enzyme for preneoplastic cells in the rat chemical hepatocarcinogenesis. Proc Natl Acad Sci U S A. 1985 Jun;82(12):3964–3968. doi: 10.1073/pnas.82.12.3964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Sharp P. A. Speculations on RNA splicing. Cell. 1981 Mar;23(3):643–646. doi: 10.1016/0092-8674(81)90425-6. [DOI] [PubMed] [Google Scholar]
  22. 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]
  23. Taylor J. B., Craig R. K., Beale D., Ketterer B. Construction and characterization of a plasmid containing complementary DNA to mRNA encoding the N-terminal amino acid sequence of the rat glutathione transferase Ya subunit. Biochem J. 1984 Apr 1;219(1):223–231. doi: 10.1042/bj2190223. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Telakowski-Hopkins C. A., Rodkey J. A., Bennett C. D., Lu A. Y., Pickett C. B. Rat liver glutathione S-transferases. Construction of a cDNA clone complementary to a Yc mRNA and prediction of the complete amino acid sequence of a Yc subunit. J Biol Chem. 1985 May 10;260(9):5820–5825. [PubMed] [Google Scholar]
  25. Tu C. P., Weiss M. J., Karakawa W. W., Reddy C. C. Cloning and sequence analysis of a cDNA plasmid for one of the rat liver glutathione S-transferase subunits. Nucleic Acids Res. 1982 Sep 25;10(18):5407–5419. doi: 10.1093/nar/10.18.5407. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Wang I. Y., Tung E., Wang A. C., Argenbright L., Wang R., Pickett C. B., Lu A. Y. Multiple Ya subunits of glutathione S-transferase detected by monoclonal antibodies. Arch Biochem Biophys. 1986 Mar;245(2):543–547. doi: 10.1016/0003-9861(86)90249-3. [DOI] [PubMed] [Google Scholar]
  27. Woo S. L. A sensitive and rapid method for recombinant phage screening. Methods Enzymol. 1979;68:389–395. doi: 10.1016/0076-6879(79)68028-x. [DOI] [PubMed] [Google Scholar]
  28. Yamada Y., Mudryj M., Sullivan M., de Crombrugghe B. Isolation and characterization of a genomic clone encoding chick alpha 1 type III collagen. J Biol Chem. 1983 Mar 10;258(5):2758–2761. [PubMed] [Google Scholar]

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