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Compensatory expression and substrate inducibility of γ-glutamyl transferase GGT2 isoform in Arabidopsis thaliana
γ-Glutamyl transferases (GGT; EC 2.3.2.2) are glutathione-degrading enzymes that are represented in Arabidopsis thaliana by a small gene family of four members. Two isoforms, GGT1 and GGT2, are apoplastic, sharing broad similarities in their amino acid sequences, but they are differently expressed i...
Autores principales: | , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Oxford University Press
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3003821/ https://www.ncbi.nlm.nih.gov/pubmed/20959624 http://dx.doi.org/10.1093/jxb/erq316 |
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author | Destro, Tiziana Prasad, Dinesh Martignago, Damiano Lliso Bernet, Ignacio Trentin, Anna Rita Renu, Indu Kumari Ferretti, Massimo Masi, Antonio |
author_facet | Destro, Tiziana Prasad, Dinesh Martignago, Damiano Lliso Bernet, Ignacio Trentin, Anna Rita Renu, Indu Kumari Ferretti, Massimo Masi, Antonio |
author_sort | Destro, Tiziana |
collection | PubMed |
description | γ-Glutamyl transferases (GGT; EC 2.3.2.2) are glutathione-degrading enzymes that are represented in Arabidopsis thaliana by a small gene family of four members. Two isoforms, GGT1 and GGT2, are apoplastic, sharing broad similarities in their amino acid sequences, but they are differently expressed in the tissues: GGT1 is expressed in roots, leaves, and siliques, while GGT2 was thought to be expressed only in siliques. It is demonstrated here that GGT2 is also expressed in wild-type roots, albeit in very small amounts. GGT2 expression is enhanced in ggt1 knockout mutants, suggesting a compensatory effect to restore GGT activity in the root apoplast. Supplementation with 100 μM glutathione (GSH) resulted in the up-regulation of GGT2 gene expression in wild-type and ggt1 knockout roots, and of GGT1 gene expression in wild-type roots. Glutathione recovery was hampered by the GGT inhibitor serine/borate, suggesting a major role for apoplastic GGTs in this process. These findings can explain the ability of ggt1 knockout mutants to retrieve exogenously added glutathione from the growth medium. |
format | Text |
id | pubmed-3003821 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-30038212010-12-20 Compensatory expression and substrate inducibility of γ-glutamyl transferase GGT2 isoform in Arabidopsis thaliana Destro, Tiziana Prasad, Dinesh Martignago, Damiano Lliso Bernet, Ignacio Trentin, Anna Rita Renu, Indu Kumari Ferretti, Massimo Masi, Antonio J Exp Bot Research Papers γ-Glutamyl transferases (GGT; EC 2.3.2.2) are glutathione-degrading enzymes that are represented in Arabidopsis thaliana by a small gene family of four members. Two isoforms, GGT1 and GGT2, are apoplastic, sharing broad similarities in their amino acid sequences, but they are differently expressed in the tissues: GGT1 is expressed in roots, leaves, and siliques, while GGT2 was thought to be expressed only in siliques. It is demonstrated here that GGT2 is also expressed in wild-type roots, albeit in very small amounts. GGT2 expression is enhanced in ggt1 knockout mutants, suggesting a compensatory effect to restore GGT activity in the root apoplast. Supplementation with 100 μM glutathione (GSH) resulted in the up-regulation of GGT2 gene expression in wild-type and ggt1 knockout roots, and of GGT1 gene expression in wild-type roots. Glutathione recovery was hampered by the GGT inhibitor serine/borate, suggesting a major role for apoplastic GGTs in this process. These findings can explain the ability of ggt1 knockout mutants to retrieve exogenously added glutathione from the growth medium. Oxford University Press 2011-01 2010-10-19 /pmc/articles/PMC3003821/ /pubmed/20959624 http://dx.doi.org/10.1093/jxb/erq316 Text en © 2010 The Author(s). This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details) |
spellingShingle | Research Papers Destro, Tiziana Prasad, Dinesh Martignago, Damiano Lliso Bernet, Ignacio Trentin, Anna Rita Renu, Indu Kumari Ferretti, Massimo Masi, Antonio Compensatory expression and substrate inducibility of γ-glutamyl transferase GGT2 isoform in Arabidopsis thaliana |
title | Compensatory expression and substrate inducibility of γ-glutamyl transferase GGT2 isoform in Arabidopsis thaliana |
title_full | Compensatory expression and substrate inducibility of γ-glutamyl transferase GGT2 isoform in Arabidopsis thaliana |
title_fullStr | Compensatory expression and substrate inducibility of γ-glutamyl transferase GGT2 isoform in Arabidopsis thaliana |
title_full_unstemmed | Compensatory expression and substrate inducibility of γ-glutamyl transferase GGT2 isoform in Arabidopsis thaliana |
title_short | Compensatory expression and substrate inducibility of γ-glutamyl transferase GGT2 isoform in Arabidopsis thaliana |
title_sort | compensatory expression and substrate inducibility of γ-glutamyl transferase ggt2 isoform in arabidopsis thaliana |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3003821/ https://www.ncbi.nlm.nih.gov/pubmed/20959624 http://dx.doi.org/10.1093/jxb/erq316 |
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