TY  - JOUR
AU  - Vidović, Marija
AU  - Battisti, Ilaria
AU  - Pantelić, Ana
AU  - Morina, Filis
AU  - Arrigoni, Giorgio
AU  - Masi, Antonio
AU  - Veljović-Jovanović, Sonja
PY  - 2022
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1574
AB  - The resurrection plant Ramonda serbica Panc. survives long desiccation periods and fully recovers metabolic functions within one day upon watering. This study aimed to identify key candidates and pathways involved in desiccation tolerance in R. serbica. We combined differential transcriptomics and proteomics, phenolic and sugar analysis, FTIR analysis of the cell wall polymers, and detailed analysis of the photosynthetic electron transport (PET) chain. The proteomic analysis allowed the relative quantification of 1192 different protein groups, of which 408 were differentially abundant between hydrated (HL) and desiccated leaves (DL). Almost all differentially abundant proteins related to photosynthetic processes were less abundant, while chlorophyll fluorescence measurements implied shifting from linear PET to cyclic electron transport (CET). The levels of H2O2 scavenging enzymes, ascorbate-glutathione cycle components, catalases, peroxiredoxins, Fe-, and Mn superoxide dismutase (SOD) were reduced in DL. However, six germin-like proteins (GLPs), four Cu/ZnSOD isoforms, three polyphenol oxidases, and 22 late embryogenesis abundant proteins (LEAPs; mainly LEA4 and dehydrins), were desiccation-inducible. Desiccation provoked cell wall remodeling related to GLP-derived H2O2/HO● activity and pectin demethylesterification. This comprehensive study contributes to understanding the role and regulation of the main metabolic pathways during desiccation aiming at crop drought tolerance improvement
PB  - MDPI
T2  - Plants
T1  - Desiccation Tolerance in Ramonda serbica Panc.: An Integrative Transcriptomic, Proteomic, Metabolite and Photosynthetic Study
IS  - 9
SP  - 1199
VL  - 11
DO  - 10.3390/plants11091199
ER  - 

@article{
author = "Vidović, Marija and Battisti, Ilaria and Pantelić, Ana and Morina, Filis and Arrigoni, Giorgio and Masi, Antonio and Veljović-Jovanović, Sonja",
year = "2022",
abstract = "The resurrection plant Ramonda serbica Panc. survives long desiccation periods and fully recovers metabolic functions within one day upon watering. This study aimed to identify key candidates and pathways involved in desiccation tolerance in R. serbica. We combined differential transcriptomics and proteomics, phenolic and sugar analysis, FTIR analysis of the cell wall polymers, and detailed analysis of the photosynthetic electron transport (PET) chain. The proteomic analysis allowed the relative quantification of 1192 different protein groups, of which 408 were differentially abundant between hydrated (HL) and desiccated leaves (DL). Almost all differentially abundant proteins related to photosynthetic processes were less abundant, while chlorophyll fluorescence measurements implied shifting from linear PET to cyclic electron transport (CET). The levels of H2O2 scavenging enzymes, ascorbate-glutathione cycle components, catalases, peroxiredoxins, Fe-, and Mn superoxide dismutase (SOD) were reduced in DL. However, six germin-like proteins (GLPs), four Cu/ZnSOD isoforms, three polyphenol oxidases, and 22 late embryogenesis abundant proteins (LEAPs; mainly LEA4 and dehydrins), were desiccation-inducible. Desiccation provoked cell wall remodeling related to GLP-derived H2O2/HO● activity and pectin demethylesterification. This comprehensive study contributes to understanding the role and regulation of the main metabolic pathways during desiccation aiming at crop drought tolerance improvement",
publisher = "MDPI",
journal = "Plants",
title = "Desiccation Tolerance in Ramonda serbica Panc.: An Integrative Transcriptomic, Proteomic, Metabolite and Photosynthetic Study",
number = "9",
pages = "1199",
volume = "11",
doi = "10.3390/plants11091199"
}

Vidović, M., Battisti, I., Pantelić, A., Morina, F., Arrigoni, G., Masi, A.,& Veljović-Jovanović, S.. (2022). Desiccation Tolerance in Ramonda serbica Panc.: An Integrative Transcriptomic, Proteomic, Metabolite and Photosynthetic Study. in Plants
MDPI., 11(9), 1199.
https://doi.org/10.3390/plants11091199

Vidović M, Battisti I, Pantelić A, Morina F, Arrigoni G, Masi A, Veljović-Jovanović S. Desiccation Tolerance in Ramonda serbica Panc.: An Integrative Transcriptomic, Proteomic, Metabolite and Photosynthetic Study. in Plants. 2022;11(9):1199.
doi:10.3390/plants11091199 .

Vidović, Marija, Battisti, Ilaria, Pantelić, Ana, Morina, Filis, Arrigoni, Giorgio, Masi, Antonio, Veljović-Jovanović, Sonja, "Desiccation Tolerance in Ramonda serbica Panc.: An Integrative Transcriptomic, Proteomic, Metabolite and Photosynthetic Study" in Plants, 11, no. 9 (2022):1199,
https://doi.org/10.3390/plants11091199 . .

TY  - JOUR
AU  - Vidović, Marija
AU  - Franchin, Cinzia
AU  - Morina, Filis
AU  - Veljović-Jovanović, Sonja
AU  - Masi, Antonio
AU  - Arrigoni, Giorgio
PY  - 2020
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1322
AB  - Resurrection plantRamonda serbicais a suitable model to investigate vegetative desiccation tolerance. However, the detailed study of these mechanisms at the protein level is hampered by the severe tissue water loss, high amount of phenolics and polysaccharide, and possible protein modifications and aggregations during the extraction and purification steps. When applied toR.serbicaleaves, widely used protein extraction protocols containing polyvinylpolypyrrolidone and ascorbate, as well as the phenol/SDS/buffer-based protocol recommended for recalcitrant plant tissues failed to eliminate persistent contamination and ensure high protein quality. Here we compared three protein extraction approaches aiming to establish the optimal one for both hydrated and desiccatedR.serbicaleaves. To evaluate the efficacy of these protocols by shotgun proteomics, we also created the firstR.serbicaannotated transcriptome database, available at. The detergent-free phenol-based extraction combined with dodecyl-beta-D-maltoside-assisted extraction enabled high-yield and high-purity protein extracts. The phenol-based protocol improved the protein-band resolution, band number, and intensity upon electrophoresis, and increased the protein yield and the number of identified peptides and protein groups by LC-MS/MS. Additionally, dodecyl-beta-D-maltoside enabled solubilisation and identification of more membrane-associated proteins. The presented study paves the way for investigating the desiccation tolerance inR.serbica, and we recommend this protocol for similar recalcitrant plant material.
PB  - Springer Heidelberg, Heidelberg
T2  - Analytical and Bioanalytical Chemistry
T1  - Efficient protein extraction for shotgun proteomics from hydrated and desiccated leaves of resurrection Ramonda serbica plants
EP  - 8312
IS  - 30
SP  - 8299
VL  - 412
DO  - 10.1007/s00216-020-02965-2
ER  - 

@article{
author = "Vidović, Marija and Franchin, Cinzia and Morina, Filis and Veljović-Jovanović, Sonja and Masi, Antonio and Arrigoni, Giorgio",
year = "2020",
abstract = "Resurrection plantRamonda serbicais a suitable model to investigate vegetative desiccation tolerance. However, the detailed study of these mechanisms at the protein level is hampered by the severe tissue water loss, high amount of phenolics and polysaccharide, and possible protein modifications and aggregations during the extraction and purification steps. When applied toR.serbicaleaves, widely used protein extraction protocols containing polyvinylpolypyrrolidone and ascorbate, as well as the phenol/SDS/buffer-based protocol recommended for recalcitrant plant tissues failed to eliminate persistent contamination and ensure high protein quality. Here we compared three protein extraction approaches aiming to establish the optimal one for both hydrated and desiccatedR.serbicaleaves. To evaluate the efficacy of these protocols by shotgun proteomics, we also created the firstR.serbicaannotated transcriptome database, available at. The detergent-free phenol-based extraction combined with dodecyl-beta-D-maltoside-assisted extraction enabled high-yield and high-purity protein extracts. The phenol-based protocol improved the protein-band resolution, band number, and intensity upon electrophoresis, and increased the protein yield and the number of identified peptides and protein groups by LC-MS/MS. Additionally, dodecyl-beta-D-maltoside enabled solubilisation and identification of more membrane-associated proteins. The presented study paves the way for investigating the desiccation tolerance inR.serbica, and we recommend this protocol for similar recalcitrant plant material.",
publisher = "Springer Heidelberg, Heidelberg",
journal = "Analytical and Bioanalytical Chemistry",
title = "Efficient protein extraction for shotgun proteomics from hydrated and desiccated leaves of resurrection Ramonda serbica plants",
pages = "8312-8299",
number = "30",
volume = "412",
doi = "10.1007/s00216-020-02965-2"
}

Vidović, M., Franchin, C., Morina, F., Veljović-Jovanović, S., Masi, A.,& Arrigoni, G.. (2020). Efficient protein extraction for shotgun proteomics from hydrated and desiccated leaves of resurrection Ramonda serbica plants. in Analytical and Bioanalytical Chemistry
Springer Heidelberg, Heidelberg., 412(30), 8299-8312.
https://doi.org/10.1007/s00216-020-02965-2

Vidović M, Franchin C, Morina F, Veljović-Jovanović S, Masi A, Arrigoni G. Efficient protein extraction for shotgun proteomics from hydrated and desiccated leaves of resurrection Ramonda serbica plants. in Analytical and Bioanalytical Chemistry. 2020;412(30):8299-8312.
doi:10.1007/s00216-020-02965-2 .

Vidović, Marija, Franchin, Cinzia, Morina, Filis, Veljović-Jovanović, Sonja, Masi, Antonio, Arrigoni, Giorgio, "Efficient protein extraction for shotgun proteomics from hydrated and desiccated leaves of resurrection Ramonda serbica plants" in Analytical and Bioanalytical Chemistry, 412, no. 30 (2020):8299-8312,
https://doi.org/10.1007/s00216-020-02965-2 . .

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 . .