首页 | 本学科首页   官方微博 | 高级检索  
   检索      


gamma-Glutamyl transpeptidase GGT4 initiates vacuolar degradation of glutathione S-conjugates in Arabidopsis
Authors:Grzam Anke  Martin Melinda N  Hell Rüdiger  Meyer Andreas J
Institution:Heidelberg Institute of Plant Sciences, University of Heidelberg, Im Neuenheimer Feld 360, Heidelberg, Germany.
Abstract: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 gamma-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.
Keywords:CHX  cycloheximide  CLSM  confocal laser scanning microscopy  Cys-B  cysteine S-bimane  CysGly-B  cysteinylglycine-bimane  GGT  γ-glutamyl-transpeptidase  GSB  glutathione S-bimane  GSH  reduced glutathione  GST  glutathione S-transferase  LMWT  low molecular weight thiol  MBB  monobromobimane  MCB  monochlorobimane  PCS  phytochelatin synthetase
本文献已被 ScienceDirect PubMed 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号