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Gene structure, expression and chromosomal localization of murine theta class glutathione transferase mGSTT1-1.

  • Research Article


Biochem. J. (1999) 337, 141–151 (Printed in Great Britain) 141 Gene structure, expression and chromosomal localization of murine Theta class glutathione transferase mGSTT1-1 Angela T. WHITTINGTON*, Vanicha VICHAI , Graham C. WEBB , Rohan T. BAKER*, William R. PEARSON and Philip G. BOARD*1 *Molecular Genetics Group, John Curtin School of Medical Research, Australian National University, P.O. Box 334, Canberra, Australian Capital Territory, 2601 Australia, Department of Biochemistry, University of Virginia, Charlottesville, VA 22908, U.S.A., and Department of Obstetrics and Gynaecology, The Queen Elizabeth Hospital, Woodville, South Australia, 5011 Australia We have isolated and characterized a cDNA and partial gene encoding a murine subfamily 1Theta class glutathione transferase (GST). The cDNA derived from mouse GSTT1 has an open reading frame of 720 bp encoding a peptide of 240 amino acids with a calculated molecular mass of 27356 Da. The encoded protein shares only 51% deduced amino acid sequence identity with mouse GSTT2, but greater than 80% deduced amino acid sequence identity with rat GSTT1 and human GSTT1. Mouse GSTT1-1 was expressed in Escherichia coli as an N-terminal 6‹ histidine-tagged protein and purified using immobilized-metal affinity chromatography on nickel-agarose. The yield of the purified recombinant protein from E. coli cultures was approx. 14 mg}l. Recombinant mouse GSTT1-1 was catalytically active towards 1,2-epoxy-3-(p-nitrophenoxy)propane, 4-nitro- benzyl chloride and dichloromethane. Low activity towards 1- menaphthyl sulphate and 1-chloro-2,4-dinitrobenzene was detec- ted, whereas mouse GSTT1-1 was inactive towards ethacrynic acid. Recombinant mouse GSTT1-1 exhibited glutathione per- oxidase activity towards cumene hydroperoxide and t-butyl hydroperoxide, but was inactive towards a range of secondary INTRODUCTION The glutathione transferases (GSTs; EC: are a family of multifunctional isoenzymes. They play a major role

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