Hgt1p, a high affinity glutathione transporter from the yeast Saccharomyces cerevisiae.

Bourbouloux, Andrée and Shahi, Puja and Chakladar, A and Delrot, Serge and Bachhawat, Anand K (2000) Hgt1p, a high affinity glutathione transporter from the yeast Saccharomyces cerevisiae. The Journal of biological chemistry, 275 (18). pp. 13259-65. ISSN 0021-9258

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Official URL: http://www.jbc.org/content/275/18/13259.long

Abstract

A high affinity glutathione transporter has been identified, cloned, and characterized from the yeast Saccharomyces cerevisiae. This transporter, Hgt1p, represents the first high affinity glutathione transporter to be described from any system so far. The strategy for the identification involved investigating candidate glutathione transporters from the yeast genome sequence project followed by genetic and physiological investigations. This approach revealed HGT1 (open reading frame YJL212c) as encoding a high affinity glutathione transporter. Yeast strains deleted in HGT1 did not show any detectable plasma membrane glutathione transport, and hgt1Delta disruptants were non-viable in a glutathione biosynthetic mutant (gsh1Delta) background. The glutathione repressible transport activity observed in wild type cells was also absent in the hgt1Delta strains. The transporter was cloned and kinetic studies indicated that Hgt1p had a high affinity for glutathione (K(m) = 54 micrometer)) and was not sensitive to competition by amino acids, dipeptides, or other tripeptides. Significant inhibition was observed, however, with oxidized glutathione and glutathione conjugates. The transporter reveals a novel class of transporters that has homologues in other yeasts and plants but with no apparent homologues in either Escherichia coli or in higher eukaryotes other than plants.

Item Type: Article
Additional Information: Copyright of this article belongs to ASBMB.
Subjects: Q Science > QD Chemistry
Depositing User: Dr. K.P.S.Sengar
Date Deposited: 02 Feb 2012 05:03
Last Modified: 19 Jan 2015 05:27
URI: http://crdd.osdd.net/open/id/eprint/832

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