γ-Glutamyl transpeptidase GGT4 initiates vacuolar degradation of glutathione S-conjugates in Arabidopsis
The xenobiotic monochlorobimane is conjugated to glutathione in the cytosol of Arabidopsis thaliana, transported to the vacuole, and hydrolyzed to cysteine S-bimane [Grzam, A., Tennstedt, P., Clemens, S., Hell, R. and Meyer, A.J. (2006) Vacuolar sequestration of glutathione S-conjugates outcompetes...
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| Main Authors: | , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
4 June 2007
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| In: |
FEBS letters
Year: 2007, Volume: 581, Issue: 17, Pages: 3131-3138 |
| ISSN: | 1873-3468 |
| DOI: | 10.1016/j.febslet.2007.05.071 |
| Online Access: | Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1016/j.febslet.2007.05.071 Verlag, kostenfrei, Volltext: http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2007.05.071/epdf |
| Author Notes: | Anke Grzam, Melinda N. Martin, Rudiger Hell, Andreas J. Meyer |
| Summary: | The xenobiotic monochlorobimane is conjugated to glutathione in the cytosol of Arabidopsis thaliana, transported to the vacuole, and hydrolyzed to cysteine S-bimane [Grzam, A., Tennstedt, P., Clemens, S., Hell, R. and Meyer, A.J. (2006) Vacuolar sequestration of glutathione S-conjugates outcompetes a possible degradation of the glutathione moiety by phytochelatin synthase. FEBS Lett. 580, 6384-6390]. The work here identifies γ-glutamyl transpeptidase 4 (At4g29210, GGT4) as the first step of vacuolar degradation of glutathione conjugates. Hydrolysis of glutathione S-bimane is blocked in ggt4 null mutants of A. thaliana. Accumulation of glutathione S-bimane in mutants and in wild-type plants treated with the high affinity GGT inhibitor acivicin shows that GGT4 is required to initiate the two step hydrolysis sequence. GGT4:green fluorescent protein fusions were used to demonstrate that GGT4 is localized in the lumen of the vacuole. |
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| Item Description: | Gesehen am 15.05.2017 |
| Physical Description: | Online Resource |
| ISSN: | 1873-3468 |
| DOI: | 10.1016/j.febslet.2007.05.071 |