Cassa di Risparmio di Padova e Rovigo (Cariparo)Fondazione Cariparo

Link to this page

Cassa di Risparmio di Padova e Rovigo (Cariparo)Fondazione Cariparo

Authors

Publications

Biochemical and quantitative proteomics investigations in Arabidopsis ggt1 mutant leaves reveal a role for the gamma-glutamyl cycle in plant's adaptation to environment

Tolin, Serena; Arrigoni, Giorgio; Trentin, Anna Rita; Veljović-Jovanović, Sonja; Pivato, Micaela; Zechmann, Bernd; Masi, Antonio

(Wiley, Hoboken, 2013)

TY  - JOUR
AU  - Tolin, Serena
AU  - Arrigoni, Giorgio
AU  - Trentin, Anna Rita
AU  - Veljović-Jovanović, Sonja
AU  - Pivato, Micaela
AU  - Zechmann, Bernd
AU  - Masi, Antonio
PY  - 2013
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/679
AB  - The existence of a gamma-glutamyl cycle consisting of intracellular GSH synthesis, extrusion to the apoplastic space and recovery by gamma-glutamyl transferase (GGT)-assisted degradation into its constituent amino acids, has been demonstrated in plants. To address the significance of this cycle in plant cells, we performed integrated biochemical, immunocytochemical, and quantitative proteomics analyses in the Arabidopsis thaliana ggt1 knockout mutant (lacking apoplastic GGT1 isoform) and its corresponding wild-type (WT). The ggt1 knockout leaves exhibited an increased ascorbate and GSH content, increased apoplastic GSH content, and enhanced protein carbonylations in the low-molecular weight range compared to WT. The combined iTRAQ and LC-MS/MS-based quantitative proteomics approach identified 70 proteins (out of 1013 identified proteins) whose abundance was significantly different in leaves of ggt1 mutant compared to WT, with a fold change 1.5. Mining of the proteome data for GSH-associated genes showed that disruption of gamma-glutamyl cycle in ggt1 knockout-leaves was associated with the induction of genes encoding four GSTs in the phi class (GSTF2, GSTF6, GSTF9, and GSTF10), a GSH peroxidase (GPX1), and glyoxylase II. Proteins with a lower abundance compared to the WT are involved in chloroplast functions, carbohydrate/maltose metabolism, and vegetative storage protein synthesis. Present findings suggest that GGT1 plays a role in redox signaling. The disruption of the gamma-glutamyl cycle in the ggt1 mutant results in pleiotropic effects related to biotic and abiotic stress response, antioxidant metabolism, senescence, carbohydrate metabolism, and photosynthesis, with strong implications for plant adaptation to the environment.
PB  - Wiley, Hoboken
T2  - Proteomics
T1  - Biochemical and quantitative proteomics investigations in Arabidopsis ggt1 mutant leaves reveal a role for the gamma-glutamyl cycle in plant's adaptation to environment
EP  - 2045
IS  - 12-13
SP  - 2031
VL  - 13
DO  - 10.1002/pmic.201200479
ER  - 
@article{
author = "Tolin, Serena and Arrigoni, Giorgio and Trentin, Anna Rita and Veljović-Jovanović, Sonja and Pivato, Micaela and Zechmann, Bernd and Masi, Antonio",
year = "2013",
abstract = "The existence of a gamma-glutamyl cycle consisting of intracellular GSH synthesis, extrusion to the apoplastic space and recovery by gamma-glutamyl transferase (GGT)-assisted degradation into its constituent amino acids, has been demonstrated in plants. To address the significance of this cycle in plant cells, we performed integrated biochemical, immunocytochemical, and quantitative proteomics analyses in the Arabidopsis thaliana ggt1 knockout mutant (lacking apoplastic GGT1 isoform) and its corresponding wild-type (WT). The ggt1 knockout leaves exhibited an increased ascorbate and GSH content, increased apoplastic GSH content, and enhanced protein carbonylations in the low-molecular weight range compared to WT. The combined iTRAQ and LC-MS/MS-based quantitative proteomics approach identified 70 proteins (out of 1013 identified proteins) whose abundance was significantly different in leaves of ggt1 mutant compared to WT, with a fold change 1.5. Mining of the proteome data for GSH-associated genes showed that disruption of gamma-glutamyl cycle in ggt1 knockout-leaves was associated with the induction of genes encoding four GSTs in the phi class (GSTF2, GSTF6, GSTF9, and GSTF10), a GSH peroxidase (GPX1), and glyoxylase II. Proteins with a lower abundance compared to the WT are involved in chloroplast functions, carbohydrate/maltose metabolism, and vegetative storage protein synthesis. Present findings suggest that GGT1 plays a role in redox signaling. The disruption of the gamma-glutamyl cycle in the ggt1 mutant results in pleiotropic effects related to biotic and abiotic stress response, antioxidant metabolism, senescence, carbohydrate metabolism, and photosynthesis, with strong implications for plant adaptation to the environment.",
publisher = "Wiley, Hoboken",
journal = "Proteomics",
title = "Biochemical and quantitative proteomics investigations in Arabidopsis ggt1 mutant leaves reveal a role for the gamma-glutamyl cycle in plant's adaptation to environment",
pages = "2045-2031",
number = "12-13",
volume = "13",
doi = "10.1002/pmic.201200479"
}
Tolin, S., Arrigoni, G., Trentin, A. R., Veljović-Jovanović, S., Pivato, M., Zechmann, B.,& Masi, A.. (2013). Biochemical and quantitative proteomics investigations in Arabidopsis ggt1 mutant leaves reveal a role for the gamma-glutamyl cycle in plant's adaptation to environment. in Proteomics
Wiley, Hoboken., 13(12-13), 2031-2045.
https://doi.org/10.1002/pmic.201200479
Tolin S, Arrigoni G, Trentin AR, Veljović-Jovanović S, Pivato M, Zechmann B, Masi A. Biochemical and quantitative proteomics investigations in Arabidopsis ggt1 mutant leaves reveal a role for the gamma-glutamyl cycle in plant's adaptation to environment. in Proteomics. 2013;13(12-13):2031-2045.
doi:10.1002/pmic.201200479 .
Tolin, Serena, Arrigoni, Giorgio, Trentin, Anna Rita, Veljović-Jovanović, Sonja, Pivato, Micaela, Zechmann, Bernd, Masi, Antonio, "Biochemical and quantitative proteomics investigations in Arabidopsis ggt1 mutant leaves reveal a role for the gamma-glutamyl cycle in plant's adaptation to environment" in Proteomics, 13, no. 12-13 (2013):2031-2045,
https://doi.org/10.1002/pmic.201200479 . .
1
50
25
49