Masi, Antonio

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  • Masi, Antonio (5)

Author's Bibliography

Mechanisms of desiccation tolerance in Ramonda serbica Panc.: transcriptomic, proteomic, metabolomic, and photosynthetic aspects

Vidović, Marija; Battisti, Ilaria; Pantelić, Ana; Morina, Filis; Arrigoni, Giorgio; Masi, Antonio; Veljović Jovanović, Sonja

(2022)

TY  - CONF
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://cherry.chem.bg.ac.rs/handle/123456789/5560
AB  - Ramonda serbica Panc. is a resurrection plant species that can survive desiccation for a long
period and fully resume metabolic functions upon rewatering in a very short period, even within
48 h. The goal of this study was to identify key candidates and pathways involved in desiccation tolerance in R. serbica. To achieve this, systems biology approach combining transcriptomics,
proteomics, and analysis of specific metabolites was employed. In addition, FTIR analysis of the
cell wall polymers and a detailed analysis of the photosynthetic electron transport (PET) chain
were performed. In total, 1192 different protein groups were quantified by TMT-based comparative quantitative proteomics. Among them, 408 protein groups showed a statistically significant
difference in abundance between hydrated (HL) and desiccated leaves (DL). Upon desiccation, the
majority of proteins related to photosynthetic processes were less abundant, while chlorophyll
fluorescence measurements implied shifting from linear photosynthetic transport (PET) to cyclic
electron transport (CET). The amounts of H2O2 scavenging enzymes, including ascorbate-glutathione cycle components, catalases, peroxiredoxins, Fe-, and Mn- superoxide dismutase (SOD) were
reduced in DL. However, four Cu/ZnSOD isoforms, three polyphenol oxidases, six germin-like proteins (GLPs), and 22 late embryogenesis abundant proteins (LEAPs; mainly LEA4 and dehydrins),
were desiccation-inducible. Desiccation-induced cell wall remodelling by changes in cell wall
polymer composition might be linked with pectin demethylesterification and GLP-derived H2O2/
HO•. Our study demonstrated that desiccation tolerance in R. serbica is a complex, species-specific process orchestrated by several metabolic pathways and regulatory networks acting at the transcript, protein, metabolite and physiological levels.
C3  - 4th International Conference on Plant Biology, Book of Abstracts
T1  - Mechanisms of desiccation tolerance in Ramonda serbica Panc.: transcriptomic, proteomic, metabolomic, and photosynthetic aspects
SP  - 27
EP  - 27
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5560
ER  - 
@conference{
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 = "Ramonda serbica Panc. is a resurrection plant species that can survive desiccation for a long
period and fully resume metabolic functions upon rewatering in a very short period, even within
48 h. The goal of this study was to identify key candidates and pathways involved in desiccation tolerance in R. serbica. To achieve this, systems biology approach combining transcriptomics,
proteomics, and analysis of specific metabolites was employed. In addition, FTIR analysis of the
cell wall polymers and a detailed analysis of the photosynthetic electron transport (PET) chain
were performed. In total, 1192 different protein groups were quantified by TMT-based comparative quantitative proteomics. Among them, 408 protein groups showed a statistically significant
difference in abundance between hydrated (HL) and desiccated leaves (DL). Upon desiccation, the
majority of proteins related to photosynthetic processes were less abundant, while chlorophyll
fluorescence measurements implied shifting from linear photosynthetic transport (PET) to cyclic
electron transport (CET). The amounts of H2O2 scavenging enzymes, including ascorbate-glutathione cycle components, catalases, peroxiredoxins, Fe-, and Mn- superoxide dismutase (SOD) were
reduced in DL. However, four Cu/ZnSOD isoforms, three polyphenol oxidases, six germin-like proteins (GLPs), and 22 late embryogenesis abundant proteins (LEAPs; mainly LEA4 and dehydrins),
were desiccation-inducible. Desiccation-induced cell wall remodelling by changes in cell wall
polymer composition might be linked with pectin demethylesterification and GLP-derived H2O2/
HO•. Our study demonstrated that desiccation tolerance in R. serbica is a complex, species-specific process orchestrated by several metabolic pathways and regulatory networks acting at the transcript, protein, metabolite and physiological levels.",
journal = "4th International Conference on Plant Biology, Book of Abstracts",
title = "Mechanisms of desiccation tolerance in Ramonda serbica Panc.: transcriptomic, proteomic, metabolomic, and photosynthetic aspects",
pages = "27-27",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5560"
}
Vidović, M., Battisti, I., Pantelić, A., Morina, F., Arrigoni, G., Masi, A.,& Veljović Jovanović, S.. (2022). Mechanisms of desiccation tolerance in Ramonda serbica Panc.: transcriptomic, proteomic, metabolomic, and photosynthetic aspects. in 4th International Conference on Plant Biology, Book of Abstracts, 27-27.
https://hdl.handle.net/21.15107/rcub_cherry_5560
Vidović M, Battisti I, Pantelić A, Morina F, Arrigoni G, Masi A, Veljović Jovanović S. Mechanisms of desiccation tolerance in Ramonda serbica Panc.: transcriptomic, proteomic, metabolomic, and photosynthetic aspects. in 4th International Conference on Plant Biology, Book of Abstracts. 2022;:27-27.
https://hdl.handle.net/21.15107/rcub_cherry_5560 .
Vidović, Marija, Battisti, Ilaria, Pantelić, Ana, Morina, Filis, Arrigoni, Giorgio, Masi, Antonio, Veljović Jovanović, Sonja, "Mechanisms of desiccation tolerance in Ramonda serbica Panc.: transcriptomic, proteomic, metabolomic, and photosynthetic aspects" in 4th International Conference on Plant Biology, Book of Abstracts (2022):27-27,
https://hdl.handle.net/21.15107/rcub_cherry_5560 .

Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves

Vidović, Marija; Stevanović, Strahinja; Franchin, Cinzia; Battisti, Ilaria; Arrigoni, Giorgio; Masi, Antonio; Veljović Jovanović, Sonja

(International Plant Proteomics Organization, 2021)

TY  - CONF
AU  - Vidović, Marija
AU  - Stevanović, Strahinja
AU  - Franchin, Cinzia
AU  - Battisti, Ilaria
AU  - Arrigoni, Giorgio
AU  - Masi, Antonio
AU  - Veljović Jovanović, Sonja
PY  - 2021
UR  - https://inppo.org/inppo2020/
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4424
AB  - Resurrection plant Ramonda serbica Panc. survives desiccation for a long period and fully recovers metabolic functions already within one day upon watering [1]. Besides osmotic stress, desiccation provokes the accelerated generation of reactive oxygen species. The aim of our study was obtaining more insight into the mechanisms of desiccation tolerance in R. serbica by TMT labelled comparative quantitative proteomics of hydrated (HL) and desiccated leaves (DL). After de novo transcriptome analysis, 189456 transcripts with 189003 unigenes were annotated with seven common databases. Proteomic analysis allowed for the relative quantification of 895 different protein groups, 321 with a statistically significant difference in abundance between FL and DL. Among them, 25% referred to chloroplast and almost the same percentage were associated with desiccation and oxidative stress. Almost all differentially abundant proteins related to photosynthetic processes were down-regulated in DL, while those required for protein translation were more abundant in HL. Within differentially abundant proteins involved in antioxidative defence, the levels of enzymes involved in ascorbate-glutathione cycle, peroxiredoxins, Fe and Mn superoxide dismutase (SOD) were all reduced in DL, while germin-like proteins, three Cu/Zn SOD isoforms and polyphenol oxidases were more abundant in DL compared with HL. The protein family with the highest number of members showing the greatest accumulation upon desiccation comprised twenty different late embryogenesis abundant proteins (LEAPs), similarly as found by differential transcriptomic analysis. Taken together, our results imply a key role of LEAPs and Cu/Zn SOD in protective mechanism against desiccation in R. serbica, that may have significant implications on drought-related studies of crops grown in arid areas. This work was supported by the Science Fund of the Republic of Serbia (PROMIS project LEAPSyn-SCI, grant number 6039663). M.V. wishes to acknowledge the support of COST Action BM1405 for approving STSM in Padua during 2017 and 2018.
PB  - International Plant Proteomics Organization
C3  - The Fourth Conference of the International Plant Proteomics Organization
T1  - Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves
SP  - 43
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4424
ER  - 
@conference{
author = "Vidović, Marija and Stevanović, Strahinja and Franchin, Cinzia and Battisti, Ilaria and Arrigoni, Giorgio and Masi, Antonio and Veljović Jovanović, Sonja",
year = "2021",
abstract = "Resurrection plant Ramonda serbica Panc. survives desiccation for a long period and fully recovers metabolic functions already within one day upon watering [1]. Besides osmotic stress, desiccation provokes the accelerated generation of reactive oxygen species. The aim of our study was obtaining more insight into the mechanisms of desiccation tolerance in R. serbica by TMT labelled comparative quantitative proteomics of hydrated (HL) and desiccated leaves (DL). After de novo transcriptome analysis, 189456 transcripts with 189003 unigenes were annotated with seven common databases. Proteomic analysis allowed for the relative quantification of 895 different protein groups, 321 with a statistically significant difference in abundance between FL and DL. Among them, 25% referred to chloroplast and almost the same percentage were associated with desiccation and oxidative stress. Almost all differentially abundant proteins related to photosynthetic processes were down-regulated in DL, while those required for protein translation were more abundant in HL. Within differentially abundant proteins involved in antioxidative defence, the levels of enzymes involved in ascorbate-glutathione cycle, peroxiredoxins, Fe and Mn superoxide dismutase (SOD) were all reduced in DL, while germin-like proteins, three Cu/Zn SOD isoforms and polyphenol oxidases were more abundant in DL compared with HL. The protein family with the highest number of members showing the greatest accumulation upon desiccation comprised twenty different late embryogenesis abundant proteins (LEAPs), similarly as found by differential transcriptomic analysis. Taken together, our results imply a key role of LEAPs and Cu/Zn SOD in protective mechanism against desiccation in R. serbica, that may have significant implications on drought-related studies of crops grown in arid areas. This work was supported by the Science Fund of the Republic of Serbia (PROMIS project LEAPSyn-SCI, grant number 6039663). M.V. wishes to acknowledge the support of COST Action BM1405 for approving STSM in Padua during 2017 and 2018.",
publisher = "International Plant Proteomics Organization",
journal = "The Fourth Conference of the International Plant Proteomics Organization",
title = "Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves",
pages = "43",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4424"
}
Vidović, M., Stevanović, S., Franchin, C., Battisti, I., Arrigoni, G., Masi, A.,& Veljović Jovanović, S.. (2021). Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves. in The Fourth Conference of the International Plant Proteomics Organization
International Plant Proteomics Organization., 43.
https://hdl.handle.net/21.15107/rcub_cherry_4424
Vidović M, Stevanović S, Franchin C, Battisti I, Arrigoni G, Masi A, Veljović Jovanović S. Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves. in The Fourth Conference of the International Plant Proteomics Organization. 2021;:43.
https://hdl.handle.net/21.15107/rcub_cherry_4424 .
Vidović, Marija, Stevanović, Strahinja, Franchin, Cinzia, Battisti, Ilaria, Arrigoni, Giorgio, Masi, Antonio, Veljović Jovanović, Sonja, "Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves" in The Fourth Conference of the International Plant Proteomics Organization (2021):43,
https://hdl.handle.net/21.15107/rcub_cherry_4424 .

Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves

Vidović, Marija; Stevanović, Strahinja; Franchin, Cinzia; Battisti, Ilaria; Arrigoni, Giorgio; Masi, Antonio; Veljović Jovanović, Sonja

(International Plant Proteomics Organization, 2021)

TY  - CONF
AU  - Vidović, Marija
AU  - Stevanović, Strahinja
AU  - Franchin, Cinzia
AU  - Battisti, Ilaria
AU  - Arrigoni, Giorgio
AU  - Masi, Antonio
AU  - Veljović Jovanović, Sonja
PY  - 2021
UR  - https://inppo.org/inppo2020/
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4842
AB  - Resurrection plant Ramonda serbica Panc. survives desiccation for a long period and fully recovers metabolic functions already within one day upon watering [1]. Besides osmotic stress, desiccation provokes the accelerated generation of reactive oxygen species. The aim of our study was obtaining more insight into the mechanisms of desiccation tolerance in R. serbica by TMT labelled comparative quantitative proteomics of hydrated (HL) and desiccated leaves (DL). After de novo transcriptome analysis, 189456 transcripts with 189003 unigenes were annotated with seven common databases. Proteomic analysis allowed for the relative quantification of 895 different protein groups, 321 with a statistically significant difference in abundance between FL and DL. Among them, 25% referred to chloroplast and almost the same percentage were associated with desiccation and oxidative stress. Almost all differentially abundant proteins related to photosynthetic processes were down-regulated in DL, while those required for protein translation were more abundant in HL. Within differentially abundant proteins involved in antioxidative defence, the levels of enzymes involved in ascorbate-glutathione cycle, peroxiredoxins, Fe and Mn superoxide dismutase (SOD) were all reduced in DL, while germin-like proteins, three Cu/Zn SOD isoforms and polyphenol oxidases were more abundant in DL compared with HL. The protein family with the highest number of members showing the greatest accumulation upon desiccation comprised twenty different late embryogenesis abundant proteins (LEAPs), similarly as found by differential transcriptomic analysis. Taken together, our results imply a key role of LEAPs and Cu/Zn SOD in protective mechanism against desiccation in R. serbica, that may have significant implications on drought-related studies of crops grown in arid areas. This work was supported by the Science Fund of the Republic of Serbia (PROMIS project LEAPSyn-SCI, grant number 6039663). M.V. wishes to acknowledge the support of COST Action BM1405 for approving STSM in Padua during 2017 and 2018.
PB  - International Plant Proteomics Organization
C3  - The Fourth Conference of the International Plant Proteomics Organization
T1  - Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves
SP  - 43
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4842
ER  - 
@conference{
author = "Vidović, Marija and Stevanović, Strahinja and Franchin, Cinzia and Battisti, Ilaria and Arrigoni, Giorgio and Masi, Antonio and Veljović Jovanović, Sonja",
year = "2021",
abstract = "Resurrection plant Ramonda serbica Panc. survives desiccation for a long period and fully recovers metabolic functions already within one day upon watering [1]. Besides osmotic stress, desiccation provokes the accelerated generation of reactive oxygen species. The aim of our study was obtaining more insight into the mechanisms of desiccation tolerance in R. serbica by TMT labelled comparative quantitative proteomics of hydrated (HL) and desiccated leaves (DL). After de novo transcriptome analysis, 189456 transcripts with 189003 unigenes were annotated with seven common databases. Proteomic analysis allowed for the relative quantification of 895 different protein groups, 321 with a statistically significant difference in abundance between FL and DL. Among them, 25% referred to chloroplast and almost the same percentage were associated with desiccation and oxidative stress. Almost all differentially abundant proteins related to photosynthetic processes were down-regulated in DL, while those required for protein translation were more abundant in HL. Within differentially abundant proteins involved in antioxidative defence, the levels of enzymes involved in ascorbate-glutathione cycle, peroxiredoxins, Fe and Mn superoxide dismutase (SOD) were all reduced in DL, while germin-like proteins, three Cu/Zn SOD isoforms and polyphenol oxidases were more abundant in DL compared with HL. The protein family with the highest number of members showing the greatest accumulation upon desiccation comprised twenty different late embryogenesis abundant proteins (LEAPs), similarly as found by differential transcriptomic analysis. Taken together, our results imply a key role of LEAPs and Cu/Zn SOD in protective mechanism against desiccation in R. serbica, that may have significant implications on drought-related studies of crops grown in arid areas. This work was supported by the Science Fund of the Republic of Serbia (PROMIS project LEAPSyn-SCI, grant number 6039663). M.V. wishes to acknowledge the support of COST Action BM1405 for approving STSM in Padua during 2017 and 2018.",
publisher = "International Plant Proteomics Organization",
journal = "The Fourth Conference of the International Plant Proteomics Organization",
title = "Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves",
pages = "43",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4842"
}
Vidović, M., Stevanović, S., Franchin, C., Battisti, I., Arrigoni, G., Masi, A.,& Veljović Jovanović, S.. (2021). Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves. in The Fourth Conference of the International Plant Proteomics Organization
International Plant Proteomics Organization., 43.
https://hdl.handle.net/21.15107/rcub_cherry_4842
Vidović M, Stevanović S, Franchin C, Battisti I, Arrigoni G, Masi A, Veljović Jovanović S. Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves. in The Fourth Conference of the International Plant Proteomics Organization. 2021;:43.
https://hdl.handle.net/21.15107/rcub_cherry_4842 .
Vidović, Marija, Stevanović, Strahinja, Franchin, Cinzia, Battisti, Ilaria, Arrigoni, Giorgio, Masi, Antonio, Veljović Jovanović, Sonja, "Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves" in The Fourth Conference of the International Plant Proteomics Organization (2021):43,
https://hdl.handle.net/21.15107/rcub_cherry_4842 .

Supplementary data for the article: 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. Anal Bioanal Chem 2020, 412 (30), 8299–8312. https://doi.org/10.1007/s00216-020-02965-2.

Vidović, Marija; Franchin, Cinzia; Morina, Filis; Veljović-Jovanović, Sonja; Masi, Antonio; Arrigoni, Giorgio

(SpringerLink, 2020)

TY  - DATA
AU  - Vidović, Marija
AU  - Franchin, Cinzia
AU  - Morina, Filis
AU  - Veljović-Jovanović, Sonja
AU  - Masi, Antonio
AU  - Arrigoni, Giorgio
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4504
PB  - SpringerLink
T2  - Analytical and Bioanalytical Chemistry
T1  - Supplementary data for the article: 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. Anal Bioanal Chem 2020, 412 (30), 8299–8312. https://doi.org/10.1007/s00216-020-02965-2.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4504
ER  - 
@misc{
author = "Vidović, Marija and Franchin, Cinzia and Morina, Filis and Veljović-Jovanović, Sonja and Masi, Antonio and Arrigoni, Giorgio",
year = "2020",
publisher = "SpringerLink",
journal = "Analytical and Bioanalytical Chemistry",
title = "Supplementary data for the article: 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. Anal Bioanal Chem 2020, 412 (30), 8299–8312. https://doi.org/10.1007/s00216-020-02965-2.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4504"
}
Vidović, M., Franchin, C., Morina, F., Veljović-Jovanović, S., Masi, A.,& Arrigoni, G.. (2020). Supplementary data for the article: 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. Anal Bioanal Chem 2020, 412 (30), 8299–8312. https://doi.org/10.1007/s00216-020-02965-2.. in Analytical and Bioanalytical Chemistry
SpringerLink..
https://hdl.handle.net/21.15107/rcub_cherry_4504
Vidović M, Franchin C, Morina F, Veljović-Jovanović S, Masi A, Arrigoni G. Supplementary data for the article: 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. Anal Bioanal Chem 2020, 412 (30), 8299–8312. https://doi.org/10.1007/s00216-020-02965-2.. in Analytical and Bioanalytical Chemistry. 2020;.
https://hdl.handle.net/21.15107/rcub_cherry_4504 .
Vidović, Marija, Franchin, Cinzia, Morina, Filis, Veljović-Jovanović, Sonja, Masi, Antonio, Arrigoni, Giorgio, "Supplementary data for the article: 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. Anal Bioanal Chem 2020, 412 (30), 8299–8312. https://doi.org/10.1007/s00216-020-02965-2." in Analytical and Bioanalytical Chemistry (2020),
https://hdl.handle.net/21.15107/rcub_cherry_4504 .

Efficient protein extraction for shotgun proteomics from hydrated and desiccated leaves of resurrection Ramonda serbica plants

Vidović, Marija; Franchin, Cinzia; Morina, Filis; Veljović-Jovanović, Sonja; Masi, Antonio; Arrigoni, Giorgio

(2020)

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://www.ncbi.nlm.nih.gov/pubmed/33037906
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4505
AB  - Resurrection plant Ramonda serbica is 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 to R. serbica leaves, 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 desiccated R. serbica leaves. To evaluate the efficacy of these protocols by shotgun proteomics, we also created the first R. serbica annotated transcriptome database, available at http://www.biomed.unipd.it/filearrigoni/Trinity_Sample_RT2.fasta . The detergent-free phenol-based extraction combined with dodecyl-β-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-β-D-maltoside enabled solubilisation and identification of more membrane-associated proteins. The presented study paves the way for investigating the desiccation tolerance in R. serbica, and we recommend this protocol for similar recalcitrant plant material.
T2  - Analytical and Bioanalytical Chemistry
T1  - Efficient protein extraction for shotgun proteomics from hydrated and desiccated leaves of resurrection Ramonda serbica plants
VL  - 412
IS  - 30
SP  - 8299
EP  - 8312
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 plant Ramonda serbica is 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 to R. serbica leaves, 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 desiccated R. serbica leaves. To evaluate the efficacy of these protocols by shotgun proteomics, we also created the first R. serbica annotated transcriptome database, available at http://www.biomed.unipd.it/filearrigoni/Trinity_Sample_RT2.fasta . The detergent-free phenol-based extraction combined with dodecyl-β-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-β-D-maltoside enabled solubilisation and identification of more membrane-associated proteins. The presented study paves the way for investigating the desiccation tolerance in R. serbica, and we recommend this protocol for similar recalcitrant plant material.",
journal = "Analytical and Bioanalytical Chemistry",
title = "Efficient protein extraction for shotgun proteomics from hydrated and desiccated leaves of resurrection Ramonda serbica plants",
volume = "412",
number = "30",
pages = "8299-8312",
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, 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 . .
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