| http://purl.uniprot.org/citations/24214398 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24214398 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24214398 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/24214398 | http://www.w3.org/2000/01/rdf-schema#comment | "Plants detoxify toxic metals through a GSH-dependent pathway. GSH homeostasis is maintained by the γ-glutamyl cycle, which involves GSH synthesis and degradation and the recycling of component amino acids. The enzyme γ-glutamyl cyclotransferase (GGCT) is involved in Glu recycling, but the gene(s) encoding GGCT has not been identified in plants. Here, we report that an Arabidopsis thaliana protein with a cation transport regulator-like domain, hereafter referred to as GGCT2;1, functions as γ-glutamyl cyclotransferase. Heterologous expression of GGCT2;1 in Saccharomyces cerevisiae produced phenotypes that were consistent with decreased GSH content attributable to either GSH degradation or the diversion of γ-glutamyl peptides to produce 5-oxoproline (5-OP). 5-OP levels were further increased by the addition of arsenite and GSH to the medium, indicating that GGCT2;1 participates in the cellular response to arsenic (As) via GSH degradation. Recombinant GGCT2;1 converted both GSH and γ-glutamyl Ala to 5-OP in vitro. GGCT2;1 transcripts were upregulated in As-treated Arabidopsis, and ggct2;1 knockout mutants were more tolerant to As and cadmium than the wild type. Overexpression of GGCT2;1 in Arabidopsis resulted in the accumulation of 5-OP. Under As toxicity, the overexpression lines showed minimal changes in de novo Glu synthesis, while the ggct2;1 mutant increased nitrogen assimilation by severalfold, resulting in a very low As/N ratio in tissue. Thus, our results suggest that GGCT2;1 ensures sufficient GSH turnover during abiotic stress by recycling Glu."xsd:string |
| http://purl.uniprot.org/citations/24214398 | http://purl.org/dc/terms/identifier | "doi:10.1105/tpc.113.111815"xsd:string |
| http://purl.uniprot.org/citations/24214398 | http://purl.org/dc/terms/identifier | "doi:10.1105/tpc.113.111815"xsd:string |
| http://purl.uniprot.org/citations/24214398 | http://purl.uniprot.org/core/author | "Dhankher O.P."xsd:string |
| http://purl.uniprot.org/citations/24214398 | http://purl.uniprot.org/core/author | "Dhankher O.P."xsd:string |
| http://purl.uniprot.org/citations/24214398 | http://purl.uniprot.org/core/author | "Chhikara S."xsd:string |
| http://purl.uniprot.org/citations/24214398 | http://purl.uniprot.org/core/author | "Chhikara S."xsd:string |
| http://purl.uniprot.org/citations/24214398 | http://purl.uniprot.org/core/author | "Coomey J."xsd:string |
| http://purl.uniprot.org/citations/24214398 | http://purl.uniprot.org/core/author | "Coomey J."xsd:string |
| http://purl.uniprot.org/citations/24214398 | http://purl.uniprot.org/core/author | "Jung H.I."xsd:string |
| http://purl.uniprot.org/citations/24214398 | http://purl.uniprot.org/core/author | "Jung H.I."xsd:string |
| http://purl.uniprot.org/citations/24214398 | http://purl.uniprot.org/core/author | "Paulose B."xsd:string |
| http://purl.uniprot.org/citations/24214398 | http://purl.uniprot.org/core/author | "Paulose B."xsd:string |
| http://purl.uniprot.org/citations/24214398 | http://purl.uniprot.org/core/author | "Vatamaniuk O."xsd:string |
| http://purl.uniprot.org/citations/24214398 | http://purl.uniprot.org/core/author | "Vatamaniuk O."xsd:string |
| http://purl.uniprot.org/citations/24214398 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/24214398 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/24214398 | http://purl.uniprot.org/core/name | "Plant Cell"xsd:string |
| http://purl.uniprot.org/citations/24214398 | http://purl.uniprot.org/core/name | "Plant Cell"xsd:string |
| http://purl.uniprot.org/citations/24214398 | http://purl.uniprot.org/core/pages | "4580-4595"xsd:string |
| http://purl.uniprot.org/citations/24214398 | http://purl.uniprot.org/core/pages | "4580-4595"xsd:string |
| http://purl.uniprot.org/citations/24214398 | http://purl.uniprot.org/core/title | "A gamma-glutamyl cyclotransferase protects Arabidopsis plants from heavy metal toxicity by recycling glutamate to maintain glutathione homeostasis."xsd:string |