The human hGSTA5 gene encodes an enzymatically active protein

Biochimica et Biophysica Acta - General Subjects

Volumn 1800, Issue 1, 2010, Pages 16-22

  Singh, Sharda P ^a   Zimniak, Ludwika ^a   Zimniak, Piotr ^a,b  

^a UNIVERSITY OF ARKANSAS FOR MEDICAL SCIENCES   (United States)

^b CENTRAL ARKANSAS VETERANS HEALTHCARE SYSTEM   (United States)

Author keywords

4 HNE; 4 hydroxynonenal; Alpha class glutathione transferase; Glutathione transferase; Lipid peroxidation; Pseudogene

Indexed keywords

4 HYDROXYNONENAL; GLUTATHIONE TRANSFERASE A5; MESSENGER RNA;

ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; GENE EXPRESSION; GENE FUNCTION; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; LIPID PEROXIDATION; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROMOTER REGION; REVERSE TRANSCRIPTION; RNA SPLICING;

ALDEHYDES; AMINO ACID SEQUENCE; BASE SEQUENCE; CATALYSIS; CELL LINE; CHROMATOGRAPHY, AFFINITY; CLONING, MOLECULAR; ELECTROPHORESIS; ESCHERICHIA COLI; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GLUTATHIONE; GLUTATHIONE TRANSFERASE; HUMANS; ISOENZYMES; K562 CELLS; MOLECULAR SEQUENCE DATA; RECOMBINANT PROTEINS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; SEQUENCE HOMOLOGY, AMINO ACID; SEQUENCE HOMOLOGY, NUCLEIC ACID; TRANSFECTION;

BACTERIA (MICROORGANISMS); EUKARYOTA;

EID: 71749101783     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2009.07.025     Document Type: Article

References (34)

1. Mannervik B., Board P.G., Hayes J.D., Listowsky I., and Pearson W.R. Nomenclature for mammalian soluble glutathione transferases. Meth. Enzymol. 401 (2005) 1-8
2. Zimniak P., and Singh S.P. Families of glutathione transferases. In: Awasthi Y.C. (Ed). Toxicology of Glutathione Transferases (2006), CRC Press, Boca Raton, FL 11-26
3. Board P.G., and Webb G.C. Isolation of a cDNA clone and localization of human glutathione S-transferase 2 genes to chromosome band 6p12. Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 2377-2381
4. Morel F., Rauch C., Coles B., Le Ferrec E., and Guillouzo A. The human glutathione transferase alpha locus: genomic organization of the gene cluster and functional characterization of the genetic polymorphism in the hGSTA1 promoter. Pharmacogenetics 12 (2002) 277-286
5. Hayes J.D., Flanagan J.U., and Jowsey I.R. Glutathione transferases. Annu. Rev. Pharmacol. Toxicol. 45 (2005) 51-88
6. Zimniak P. Substrates and reaction mechanisms of GSTs. In: Awasthi Y.C. (Ed). Toxicology of Glutathione Transferases (2006), CRC Press, Boca Raton, FL 71-101
7. Coles B.F., and Kadlubar F.F. Human alpha class glutathione S-transferases: genetic polymorphism, expression, and susceptibility to disease. Meth. Enzymol. 401 (2005) 9-42
8. Kozak M. Initiation of translation in prokaryotes and eukaryotes. Gene 234 (1999) 187-208
9. Simons P.C., and Vander Jagt D.L. Purification of glutathione S-transferases from human liver by glutathione-affinity chromatography. Anal. Biochem. 82 (1977) 334-341
10. Singh S.P., Coronella J.A., Beneš H., Cochrane B.J., and Zimniak P. Catalytic function of Drosophila melanogaster glutathione S-transferase DmGSTS1-1 (GST-2) in conjugation of lipid peroxidation end products. Eur. J. Biochem. 268 (2001) 2912-2923
11. Kapust R.B., and Waugh D.S. Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci. 8 (1999) 1668-1674
12. Hartman J., Daram P., Frizzell R.A., Rado T., Benos D.J., and Sorscher E.J. Affinity purification of insoluble recombinant fusion proteins containing glutathione-S-transferase. Biotechnol. Bioeng. 39 (1992) 828-832
13. Kagawa N., and Cao Q. Osmotic stress induced by carbohydrates enhances expression of foreign proteins in Escherichia coli. Arch. Biochem. Biophys. 393 (2001) 290-296
14. Yasukawa T., Kanei-Ishii C., Maekawa T., Fujimoto J., Yamamoto T., and Ishii S. Increase of solubility of foreign proteins in Escherichia coli by coproduction of the bacterial thioredoxin. J. Biol. Chem. 270 (1995) 25328-25331
15. Ghosh S., Rasheedi S., Rahim S.S., Banerjee S., Choudhary R.K., Chakhaiyar P., Ehtesham N.Z., Mukhopadhyay S., and Hasnain S.E. Method for enhancing solubility of the expressed recombinant proteins in Escherichia coli. Biotechniques 37 (2004) 418, 420, 422-413
16. Weickert M.J., Doherty D.H., Best E.A., and Olins P.O. Optimization of heterologous protein production in Escherichia coli. Curr. Opin. Biotechnol. 7 (1996) 494-499
17. Widersten M. Heterologous expression in Escherichia coli of soluble active-site random mutants of haloalkane dehalogenase from Xanthobacter autotrophicus GJ10 by coexpression of molecular chaperonins GroEL/ES. Protein Expr. Purif. 13 (1998) 389-395
18. Galloway C.A., Sowden M.P., and Smith H.C. Increasing the yield of soluble recombinant protein expressed in E. coli by induction during late log phase. Biotechniques 34 (2003) 524-530
19. Hubatsch I., Ridderstrom M., and Mannervik B. Human glutathione transferase A4-4: an Alpha class enzyme with high catalytic efficiency in the conjugation of 4-hydroxynonenal and other genotoxic products of lipid peroxidation. Biochem. J. 330 (1998) 175-179
20. Singh S.P., Janecki A.J., Srivastava S.K., Awasthi S., Awasthi Y.C., Xia S.J., and Zimniak P. Membrane association of glutathione S-transferase mGSTA4-4, an enzyme that metabolizes lipid peroxidation products. J. Biol. Chem. 277 (2002) 4232-4239
21. Nanduri B., Hayden J.B., Awasthi Y.C., and Zimniak P. Amino acid residue 104 in an alpha-class glutathione S-transferase is essential for the high selectivity and specificity of the enzyme for 4-hydroxynonenal. Arch. Biochem. Biophys. 335 (1996) 305-310
22. Ayyadevara S., Engle M.R., Singh S.P., Dandapat A., Lichti C.F., Beneš H., Shmookler Reis R.J., Liebau E., and Zimniak P. Lifespan and stress resistance of Caenorhabditis elegans are increased by expression of glutathione transferases capable of metabolizing the lipid peroxidation product 4-hydroxynonenal. Aging Cell 4 (2005) 257-271
23. Sawicki R., Singh S.P., Mondal A.K., Beneš H., and Zimniak P. Cloning, expression, and biochemical characterization of one Epsilon-class (GST-3) and ten Delta-class (GST-1) glutathione S-transferases from Drosophila melanogaster, and identification of additional nine members of the Epsilon class. Biochem. J. 370 (2003) 661-669
24. Ayyadevara S., Dandapat A., Singh S.P., Siegel E.R., Shmookler Reis R.J., Zimniak L., and Zimniak P. Life span and stress resistance of Caenorhabditis elegans are differentially affected by glutathione transferases metabolizing 4-hydroxynon-2-enal. Mech. Ageing Dev. 128 (2007) 196-205
25. Zimniak P. Detoxification reactions: relevance to aging. Ageing Res. Rev. 7 (2008) 281-300
26. Sinning I., Kleywegt G.J., Cowan S.W., Reinemer P., Dirr H.W., Huber R., Gilliland G.L., Armstrong R.N., Ji X., Board P.G., Olin B., Mannervik B., and Jones T.A. Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the mu and pi class enzymes. J. Mol. Biol. 232 (1993) 192-212
27. Grahn E., Novotny M., Jakobsson E., Gustafsson A., Grehn L., Olin B., Madsen D., Wahlberg M., Mannervik B., and Kleywegt G.J. New crystal structures of human glutathione transferase A1-1 shed light on glutathione binding and the conformation of the C-terminal helix. Acta Cryst. 62D (2006) 197-207
28. Bjornestedt R., Stenberg G., Widersten M., Board P.G., Sinning I., Jones T.A., and Mannervik B. Functional significance of arginine 15 in the active site of human alpha glutathione transferase A1-1. J. Mol. Biol. 247 (1995) 765-773
29. Nilsson L.O., Gustafsson A., and Mannervik B. Redesign of substrate-selectivity determining modules of glutathione transferase A1-1 installs high catalytic efficiency with toxic alkenal products of lipid peroxidation. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 9408-9412
30. Bjornestedt R., Tardioli S., and Mannervik B. The high activity of rat glutathione transferase 8-8 with alkene substrates is dependent on a glycine residue in the active site. J. Biol. Chem. 270 (1995) 29705-29709
31. Bruns C.M., Hubatsch I., Ridderstrom M., Mannervik B., and Tainer J.A. Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products. J. Mol. Biol. 288 (1999) 427-439
32. Coles B.F., Anderson K.E., Doerge D.R., Churchwell M.I., Lang N.P., and Kadlubar F.F. Quantitative analysis of interindividual variation of glutathione S-transferase expression in human pancreas and the ambiguity of correlating genotype with phenotype. Cancer Res. 60 (2000) 573-579
33. Chamary J.V., Parmley J.L., and Hurst L.D. Hearing silence: non-neutral evolution at synonymous sites in mammals. Nat. Rev. Genet. 7 (2006) 98-108
34. Tsai C.J., Sauna Z.E., Kimchi-Sarfaty C., Ambudkar S.V., Gottesman M.M., and Nussinov R. Synonymous mutations and ribosome stalling can lead to altered folding pathways and distinct minima. J. Mol. Biol. 383 (2008) 281-291