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J Biol Chem, Vol. 273, Issue 45, 29915-29922, November 6, 1998
From the Department of Biological Sciences, St. John's University,
Jamaica, New York 11439
The glutathione S-transferases (GSTs)
represent a significant group of detoxification enzymes that play an
important role in drug resistance in all eukaryotic species. In this
paper we report an identification and characterization of the two
Saccharomyces cerevisiae genes, GTT1 and
GTT2 (glutathione
transferase 1 and 2), coding for functional GST enzymes.
Despite only limited similarity with GSTs from other organisms
(~50%), recombinant Gtt1p and Gtt2p exhibit GST activity with
1-chloro-2,4-dinitrobenzene as a substrate. Both Gtt1p and Gtt2p are
able to form homodimers, as determined by two hybrid assay. Subcellular
fractionation demonstrated that Gtt1p associates with the endoplasmic
reticulum. Expression of GTT1 is induced after diauxic
shift and remains high throughout the stationary phase. Strains deleted
for GTT1 and/or GTT2 are viable but exhibit
increased sensitivity to heat shock in stationary phase and limited
ability to grow at 39 °C.
A Novel Membrane-bound Glutathione S-Transferase
Functions in the Stationary Phase of the Yeast Saccharomyces
cerevisiae
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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