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. 1998 Aug 1;333(Pt 3):735–739. doi: 10.1042/bj3330735

Amino acid sequence of glutathione S-transferase rGSTM5* from rat testis.

M F Tam 1, C H Hsieh 1, S P Tsai 1, T C Tam 1
PMCID: PMC1219639  PMID: 9677335

Abstract

Glutathione S-transferase rGSTM5* was isolated from rat testis with a combination of glutathione affinity column and reverse-phase column chromatography. The protein was digested with Achromobacter protease I or endoproteinase Arg-C. The peptide fragments were isolated for electrospray MS and N-terminal peptide sequencing analyses. The primary amino acid sequence of rGSTM5* comprises 217 residues and has a calculated average molecular mass of 25495.3 Da. The result is identical to that obtained for rGSTM5* with liquid chromatography-MS from a mixture of rat testicular GSTs. Therefore, rGSTM5* has not been post-translationally modified.

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Selected References

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  1. Abramovitz M., Listowsky I. Selective expression of a unique glutathione S-transferase Yb3 gene in rat brain. J Biol Chem. 1987 Jun 5;262(16):7770–7773. [PubMed] [Google Scholar]
  2. Alin P., Jensson H., Cederlund E., Jörnvall H., Mannervik B. Cytosolic glutathione transferases from rat liver. Primary structure of class alpha glutathione transferase 8-8 and characterization of low-abundance class Mu glutathione transferases. Biochem J. 1989 Jul 15;261(2):531–539. doi: 10.1042/bj2610531. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Alin P., Mannervik B., Jörnvall H. Cytosolic rat liver glutathione transferase 4-4. Primary structure of the protein reveals extensive differences between homologous glutathione transferases of classes alpha and mu. Eur J Biochem. 1986 Apr 15;156(2):343–350. doi: 10.1111/j.1432-1033.1986.tb09588.x. [DOI] [PubMed] [Google Scholar]
  4. Armstrong R. N. Glutathione S-transferases: reaction mechanism, structure, and function. Chem Res Toxicol. 1991 Mar-Apr;4(2):131–140. doi: 10.1021/tx00020a001. [DOI] [PubMed] [Google Scholar]
  5. Bhargava M. M., Listowsky I., Arias I. M. Ligandin. Bilirubin binding and glutathione-S-transferase activity are independent processes. J Biol Chem. 1978 Jun 25;253(12):4112–4115. [PubMed] [Google Scholar]
  6. Christ-Hazelhof E., Nugteren D. H. Purification and characterisation of prostaglandin endoperoxide D-isomerase, a cytoplasmic, glutathione-requiring enzyme. Biochim Biophys Acta. 1979 Jan 29;572(1):43–51. doi: 10.1016/0005-2760(79)90198-x. [DOI] [PubMed] [Google Scholar]
  7. Hayes J. D., Pulford D. J. The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit Rev Biochem Mol Biol. 1995;30(6):445–600. doi: 10.3109/10409239509083491. [DOI] [PubMed] [Google Scholar]
  8. Hsieh C. H., Tsai S. P., Yeh H. I., Sheu T. C., Tam M. F. Mass spectrometric analysis of rat ovary and testis cytosolic glutathione S-transferases (GSTs): identification of a novel class-alpha GST, rGSTA6*, in rat testis. Biochem J. 1997 Apr 15;323(Pt 2):503–510. doi: 10.1042/bj3230503. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Ishigaki S., Abramovitz M., Listowsky I. Glutathione-S-transferases are major cytosolic thyroid hormone binding proteins. Arch Biochem Biophys. 1989 Sep;273(2):265–272. doi: 10.1016/0003-9861(89)90483-9. [DOI] [PubMed] [Google Scholar]
  10. Ishikawa T., Tsuchida S., Satoh K., Sato K. The subunit structure of a major glutathione S-transferase form, MT, in rat testis. Evidence for a heterodimer consisting of subunits with different isoelectric points. Eur J Biochem. 1988 Oct 1;176(3):551–557. doi: 10.1111/j.1432-1033.1988.tb14313.x. [DOI] [PubMed] [Google Scholar]
  11. Ji X., Johnson W. W., Sesay M. A., Dickert L., Prasad S. M., Ammon H. L., Armstrong R. N., Gilliland G. L. Structure and function of the xenobiotic substrate binding site of a glutathione S-transferase as revealed by X-ray crystallographic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene. Biochemistry. 1994 Feb 8;33(5):1043–1052. doi: 10.1021/bi00171a002. [DOI] [PubMed] [Google Scholar]
  12. Ji X., Zhang P., Armstrong R. N., Gilliland G. L. The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2-A resolution. Biochemistry. 1992 Oct 27;31(42):10169–10184. doi: 10.1021/bi00157a004. [DOI] [PubMed] [Google Scholar]
  13. Johnson J. A., Finn K. A., Siegel F. L. Tissue distribution of enzymic methylation of glutathione S-transferase and its effects on catalytic activity. Methylation of glutathione S-transferase 11-11 inhibits conjugating activity towards 1-chloro-2,4-dinitrobenzene. Biochem J. 1992 Feb 15;282(Pt 1):279–289. doi: 10.1042/bj2820279. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Johnson W. W., Liu S., Ji X., Gilliland G. L., Armstrong R. N. Tyrosine 115 participates both in chemical and physical steps of the catalytic mechanism of a glutathione S-transferase. J Biol Chem. 1993 Jun 5;268(16):11508–11511. [PubMed] [Google Scholar]
  15. Lai H. C., Grove G., Tu C. P. Cloning and sequence analysis of a cDNA for a rat liver glutathione S-transferase Yb subunit. Nucleic Acids Res. 1986 Aug 11;14(15):6101–6114. doi: 10.1093/nar/14.15.6101. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Lai H. C., Qian B., Grove G., Tu C. P. Gene expression of rat glutathione S-transferases. Evidence for gene conversion in the evolution of the Yb multigene family. J Biol Chem. 1988 Aug 15;263(23):11389–11395. [PubMed] [Google Scholar]
  17. Lai H. C., Tu C. P. Rat glutathione S-transferases supergene family. Characterization of an anionic Yb subunit cDNA clone. J Biol Chem. 1986 Oct 15;261(29):13793–13799. [PubMed] [Google Scholar]
  18. Liu L. F., Liaw Y. C., Tam M. F. Characterization of chicken-liver glutathione S-transferase (GST) A1-1 and A2-2 isoenzymes and their site-directed mutants heterologously expressed in Escherichia coli: identification of Lys-15 and Ser-208 on cGSTA1-1 as residues interacting with ethacrynic acid. Biochem J. 1997 Oct 15;327(Pt 2):593–600. doi: 10.1042/bj3270593. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Mannervik B., Awasthi Y. C., Board P. G., Hayes J. D., Di Ilio C., Ketterer B., Listowsky I., Morgenstern R., Muramatsu M., Pearson W. R. Nomenclature for human glutathione transferases. Biochem J. 1992 Feb 15;282(Pt 1):305–306. doi: 10.1042/bj2820305. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Mannervik B., Danielson U. H. Glutathione transferases--structure and catalytic activity. CRC Crit Rev Biochem. 1988;23(3):283–337. doi: 10.3109/10409238809088226. [DOI] [PubMed] [Google Scholar]
  21. Shan S., Armstrong R. N. Rational reconstruction of the active site of a class mu glutathione S-transferase. J Biol Chem. 1994 Dec 23;269(51):32373–32379. [PubMed] [Google Scholar]
  22. Simons P. C., Vander Jagt D. L. Purification of glutathione S-transferases by glutathione-affinity chromatography. Methods Enzymol. 1981;77:235–237. doi: 10.1016/s0076-6879(81)77031-9. [DOI] [PubMed] [Google Scholar]
  23. Tan K. H., Meyer D. J., Coles B., Ketterer B. Thymine hydroperoxide, a substrate for rat Se-dependent glutathione peroxidase and glutathione transferase isoenzymes. FEBS Lett. 1986 Oct 27;207(2):231–233. doi: 10.1016/0014-5793(86)81494-6. [DOI] [PubMed] [Google Scholar]
  24. Taniguchi H., Pyerin W. Glutathione S-transferase is an in vitro substrate of Ca++-phospholipid-dependent protein kinase (protein kinase C). Biochem Biophys Res Commun. 1989 Aug 15;162(3):903–907. doi: 10.1016/0006-291x(89)90757-2. [DOI] [PubMed] [Google Scholar]
  25. Tsuchida S., Sato K. Glutathione transferases and cancer. Crit Rev Biochem Mol Biol. 1992;27(4-5):337–384. doi: 10.3109/10409239209082566. [DOI] [PubMed] [Google Scholar]
  26. Yeh H. I., Hsieh C. H., Wang L. Y., Tsai S. P., Hsu H. Y., Tam M. F. Mass spectrometric analysis of rat liver cytosolic glutathione S-transferases: modifications are limited to N-terminal processing. Biochem J. 1995 May 15;308(Pt 1):69–75. doi: 10.1042/bj3080069. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Yeh H., Lee J., Tsai S., Hsieh C., Tam M. F. Rat kidney glutathione S-transferase 1 subunits have C-terminal truncations. Biochem J. 1996 Mar 15;314(Pt 3):1017–1025. doi: 10.1042/bj3141017. [DOI] [PMC free article] [PubMed] [Google Scholar]

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