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Journal of Bacteriology, August 2009, p. 5196-5204, Vol. 191, No. 16
0021-9193/09/$08.00+0 doi:10.1128/JB.00297-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.
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Department of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Received 5 March 2009/ Accepted 2 June 2009
Halophilic archaea were found to contain in their cytoplasm millimolar concentrations of
-glutamylcysteine (
GC) instead of glutathione. Previous analysis of the genome sequence of the archaeon Halobacterium sp. strain NRC-1 has indicated the presence of a sequence homologous to sequences known to encode the glutamate-cysteine ligase GshA. We report here the identification of the gshA gene in the extremely halophilic archaeon Haloferax volcanii and show that H. volcanii gshA directs in vivo the synthesis and accumulation of
GC. We also show that the H. volcanii gene when expressed in an Escherichia coli strain lacking functional GshA is able to restore synthesis of glutathione.
Published ahead of print on 12 June 2009.
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