TY  - CONF
AU  - Pantelic, Ana
AU  - Stevanovic, Strahinja
AU  - Milić Komić, Sonja
AU  - Kilibarda, Nataša
AU  - Vidović, Marija
PY  - 2023
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/3087
AB  - Ramonda serbica Panc. is an ancient resurrection plant, that survives a long desiccation period and fully recovers metabolic functions upon watering. The main characteristic of desiccationtolerant plant species is their ability to accumulate protective late embryogenesis abounded protein (LEAPs). To propose their role in R. serbica desiccation tolerance we structurally analysed LEAPs in hydrated and desiccated leaves. According to transcriptomics, 318 LEAPs were identified and classified into seven family groups based on protein BLAST analysis and conserved motifs (Pfam). The largest LEAPs belonged to the LEA2 and LEA4 protein family groups. We employed online tools to analyse physicochemical characteristics (Expasy, ProtParam, BioPython, GRAVY calculator), disorder propensity, and characterization protein structures (FELLS, JPred, SOPMA, PsiPred, Phyre2, Espritz-DisProt, Espritz-X, Iupred, TMHMM, +Heliquest). The most abundant, atypical LEA2 group containing 127, mostly hydrophobic proteins, was divided into five subgroups. Members of this group were predicted to fold into globular domains, β-barrel at the C-terminus, followed by transmembrane hydrophobic-helices and disordered N-terminal regions. Results indicated the possible involvement in the protection of the chloroplastic membranes. The LEA4 group exhibited an exceptionally high tendency to form amphipathic α-helices and simultaneously had a high disorder propensity. This group is made of 96 proteins, classified into 3 subgroups. The high content of polar and charged amino acids (lysine, glutamate, and aspartate) is characteristic of this group. Motifs corresponding to the R. serbica LEA4 protein family group folded into A-type α-helices that contained positive, negative, and hydrophobic surfaces. Based on previous knowledge, the possible functions of the LEA2 and LEA4 groups are discussed with significant implications on cell preservation technology and the improvement of crop drought tolerance.
PB  - Belgrade : Institute of molecular genetics and genetic engineering
C3  - 4th Belgrade Bioinformatics Conference, 2023, 4, 68-68
T1  - Two contrasting late embryogenesis abounded protein family groups of Ramonda serbica Panc.
SP  - 68
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_3087
ER  - 

@conference{
author = "Pantelic, Ana and Stevanovic, Strahinja and Milić Komić, Sonja and Kilibarda, Nataša and Vidović, Marija",
year = "2023",
abstract = "Ramonda serbica Panc. is an ancient resurrection plant, that survives a long desiccation period and fully recovers metabolic functions upon watering. The main characteristic of desiccationtolerant plant species is their ability to accumulate protective late embryogenesis abounded protein (LEAPs). To propose their role in R. serbica desiccation tolerance we structurally analysed LEAPs in hydrated and desiccated leaves. According to transcriptomics, 318 LEAPs were identified and classified into seven family groups based on protein BLAST analysis and conserved motifs (Pfam). The largest LEAPs belonged to the LEA2 and LEA4 protein family groups. We employed online tools to analyse physicochemical characteristics (Expasy, ProtParam, BioPython, GRAVY calculator), disorder propensity, and characterization protein structures (FELLS, JPred, SOPMA, PsiPred, Phyre2, Espritz-DisProt, Espritz-X, Iupred, TMHMM, +Heliquest). The most abundant, atypical LEA2 group containing 127, mostly hydrophobic proteins, was divided into five subgroups. Members of this group were predicted to fold into globular domains, β-barrel at the C-terminus, followed by transmembrane hydrophobic-helices and disordered N-terminal regions. Results indicated the possible involvement in the protection of the chloroplastic membranes. The LEA4 group exhibited an exceptionally high tendency to form amphipathic α-helices and simultaneously had a high disorder propensity. This group is made of 96 proteins, classified into 3 subgroups. The high content of polar and charged amino acids (lysine, glutamate, and aspartate) is characteristic of this group. Motifs corresponding to the R. serbica LEA4 protein family group folded into A-type α-helices that contained positive, negative, and hydrophobic surfaces. Based on previous knowledge, the possible functions of the LEA2 and LEA4 groups are discussed with significant implications on cell preservation technology and the improvement of crop drought tolerance.",
publisher = "Belgrade : Institute of molecular genetics and genetic engineering",
journal = "4th Belgrade Bioinformatics Conference, 2023, 4, 68-68",
title = "Two contrasting late embryogenesis abounded protein family groups of Ramonda serbica Panc.",
pages = "68",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_3087"
}

Pantelic, A., Stevanovic, S., Milić Komić, S., Kilibarda, N.,& Vidović, M.. (2023). Two contrasting late embryogenesis abounded protein family groups of Ramonda serbica Panc.. in 4th Belgrade Bioinformatics Conference, 2023, 4, 68-68
Belgrade : Institute of molecular genetics and genetic engineering., 68.
https://hdl.handle.net/21.15107/rcub_rimsi_3087

Pantelic A, Stevanovic S, Milić Komić S, Kilibarda N, Vidović M. Two contrasting late embryogenesis abounded protein family groups of Ramonda serbica Panc.. in 4th Belgrade Bioinformatics Conference, 2023, 4, 68-68. 2023;:68.
https://hdl.handle.net/21.15107/rcub_rimsi_3087 .

Pantelic, Ana, Stevanovic, Strahinja, Milić Komić, Sonja, Kilibarda, Nataša, Vidović, Marija, "Two contrasting late embryogenesis abounded protein family groups of Ramonda serbica Panc." in 4th Belgrade Bioinformatics Conference, 2023, 4, 68-68 (2023):68,
https://hdl.handle.net/21.15107/rcub_rimsi_3087 .

TY  - JOUR
AU  - Milić Komić, Sonja
AU  - Veljović-Jovanović, Sonja
AU  - Pantelic, Ana
AU  - Vidović, Marija
PY  - 2022
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/2900
AB  - Ressurection plants are extraordinary because of their ability to withstand long periods without water, enter a state of anhydrobiosis, and fully recover upon water arrival. Ramonda serbica Panč. is a relic and endemic species that belongs to a very small group of desiccation-tolerant plants in Europe. Underlying physiological, molecular and morphological mechanisms that enable these plants to survive harsh environmental conditions have been an appealing subject of many researchers. Most of the genes responsible for this amazing ability are present in other plants, and research of those genes which could be activated in crops is growing much more attention because of the imminent crisis regarding food supplies in the near future. Key components involved in the response to dehydration in R. serbica plants were analysed through a comprehensive transcriptomic, proteomic, metabolite and photosynthetic study. Late embryogenesis abundant proteins play a significant role in the complex defence processes involved in desiccation tolerance. Defining LEAPs physicochemical characteristics and specific physiological functions may lead us to their applicability in other areas of research.
PB  - Novi Sad : Faculty of Sciences, Department of Biology
T2  - Biologia Serbica
T1  - Structural characterisation of late embryogenesis abundant proteins in Ramonda serbica Panč.
EP  - 66
IS  - 44
SP  - 59
VL  - 1
DO  - 10.5281/zenodo.7075212
ER  - 

@article{
author = "Milić Komić, Sonja and Veljović-Jovanović, Sonja and Pantelic, Ana and Vidović, Marija",
year = "2022",
abstract = "Ressurection plants are extraordinary because of their ability to withstand long periods without water, enter a state of anhydrobiosis, and fully recover upon water arrival. Ramonda serbica Panč. is a relic and endemic species that belongs to a very small group of desiccation-tolerant plants in Europe. Underlying physiological, molecular and morphological mechanisms that enable these plants to survive harsh environmental conditions have been an appealing subject of many researchers. Most of the genes responsible for this amazing ability are present in other plants, and research of those genes which could be activated in crops is growing much more attention because of the imminent crisis regarding food supplies in the near future. Key components involved in the response to dehydration in R. serbica plants were analysed through a comprehensive transcriptomic, proteomic, metabolite and photosynthetic study. Late embryogenesis abundant proteins play a significant role in the complex defence processes involved in desiccation tolerance. Defining LEAPs physicochemical characteristics and specific physiological functions may lead us to their applicability in other areas of research.",
publisher = "Novi Sad : Faculty of Sciences, Department of Biology",
journal = "Biologia Serbica",
title = "Structural characterisation of late embryogenesis abundant proteins in Ramonda serbica Panč.",
pages = "66-59",
number = "44",
volume = "1",
doi = "10.5281/zenodo.7075212"
}

Milić Komić, S., Veljović-Jovanović, S., Pantelic, A.,& Vidović, M.. (2022). Structural characterisation of late embryogenesis abundant proteins in Ramonda serbica Panč.. in Biologia Serbica
Novi Sad : Faculty of Sciences, Department of Biology., 1(44), 59-66.
https://doi.org/10.5281/zenodo.7075212

Milić Komić S, Veljović-Jovanović S, Pantelic A, Vidović M. Structural characterisation of late embryogenesis abundant proteins in Ramonda serbica Panč.. in Biologia Serbica. 2022;1(44):59-66.
doi:10.5281/zenodo.7075212 .

Milić Komić, Sonja, Veljović-Jovanović, Sonja, Pantelic, Ana, Vidović, Marija, "Structural characterisation of late embryogenesis abundant proteins in Ramonda serbica Panč." in Biologia Serbica, 1, no. 44 (2022):59-66,
https://doi.org/10.5281/zenodo.7075212 . .

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  - CONF
AU  - Milić Komić, Sonja
AU  - Veljović-Jovanović, Sonja
AU  - Pantelic, Ana
AU  - Vidović, Marija
PY  - 2022
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/3086
AB  - Ressurection plants are extraordinary because of their ability to withstand long periods without water, enter a state of anhydrobiosis, and fully recover upon water arrival. Ramonda serbica is a relic and endemic species that belong to a very small group of desiccation-tolerant plants in Europe. Underlying physiological, molecular and morphological mechanisms that enable these plants to survive harsh environmental conditions have been an appealing subject to many researchers. Most of the genes responsible for this amazing ability are present in other plants, and this path of research where those genes could be activated in crops is growing much more attention because of the imminent crisis regarding food supplies in the near future. Key components involved in the response to dehydration in R. serbica plants were analysed through a comprehensive transcriptomic, proteomic, metabolite and photosynthetic study. Late embryogenesis abundant proteins play a significant role in the complex defence processes involved in desiccation tolerance. Defining physicochemical characteristics and specific physiological functions of late embryogenesis abundant proteins – LEAPs may lead to their applicability in other areas of research.
PB  - Belgrade : Faculty of Chemistry, Serbian Biochemical Society
C3  - Serbian Biochemical Society Eleventh Conference (scientific meeting of an international character) - "Amazing Biochemistry"
T1  - Late embryogenesis abundant proteins: Structural characterisation and interaction with α-synuclein
SP  - 37
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_3086
ER  - 

@conference{
author = "Milić Komić, Sonja and Veljović-Jovanović, Sonja and Pantelic, Ana and Vidović, Marija",
year = "2022",
abstract = "Ressurection plants are extraordinary because of their ability to withstand long periods without water, enter a state of anhydrobiosis, and fully recover upon water arrival. Ramonda serbica is a relic and endemic species that belong to a very small group of desiccation-tolerant plants in Europe. Underlying physiological, molecular and morphological mechanisms that enable these plants to survive harsh environmental conditions have been an appealing subject to many researchers. Most of the genes responsible for this amazing ability are present in other plants, and this path of research where those genes could be activated in crops is growing much more attention because of the imminent crisis regarding food supplies in the near future. Key components involved in the response to dehydration in R. serbica plants were analysed through a comprehensive transcriptomic, proteomic, metabolite and photosynthetic study. Late embryogenesis abundant proteins play a significant role in the complex defence processes involved in desiccation tolerance. Defining physicochemical characteristics and specific physiological functions of late embryogenesis abundant proteins – LEAPs may lead to their applicability in other areas of research.",
publisher = "Belgrade : Faculty of Chemistry, Serbian Biochemical Society",
journal = "Serbian Biochemical Society Eleventh Conference (scientific meeting of an international character) - "Amazing Biochemistry"",
title = "Late embryogenesis abundant proteins: Structural characterisation and interaction with α-synuclein",
pages = "37",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_3086"
}

Milić Komić, S., Veljović-Jovanović, S., Pantelic, A.,& Vidović, M.. (2022). Late embryogenesis abundant proteins: Structural characterisation and interaction with α-synuclein. in Serbian Biochemical Society Eleventh Conference (scientific meeting of an international character) - "Amazing Biochemistry"
Belgrade : Faculty of Chemistry, Serbian Biochemical Society., 37.
https://hdl.handle.net/21.15107/rcub_rimsi_3086

Milić Komić S, Veljović-Jovanović S, Pantelic A, Vidović M. Late embryogenesis abundant proteins: Structural characterisation and interaction with α-synuclein. in Serbian Biochemical Society Eleventh Conference (scientific meeting of an international character) - "Amazing Biochemistry". 2022;:37.
https://hdl.handle.net/21.15107/rcub_rimsi_3086 .

Milić Komić, Sonja, Veljović-Jovanović, Sonja, Pantelic, Ana, Vidović, Marija, "Late embryogenesis abundant proteins: Structural characterisation and interaction with α-synuclein" in Serbian Biochemical Society Eleventh Conference (scientific meeting of an international character) - "Amazing Biochemistry" (2022):37,
https://hdl.handle.net/21.15107/rcub_rimsi_3086 .

TY  - CONF
AU  - Pantelic, Ana
AU  - Stevanovic, Strahinja
AU  - Milić, Dejana
AU  - Milić Komić, Sonja
AU  - Kilibarda, Nataša
AU  - Vidović, Marija
PY  - 2022
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/3085
AB  - An ancient resurrection plant Ramonda serbica Panc. is able to survive a long desiccation period and reestablish metabolic activity upon watering. A hallmark of desiccation tolerance in the resurrection species is the accumulation of protective late embryogenesis abundant proteins (LEAPs). These intrinsically disordered proteins (IDPs) may stabilize the correct structure of proteins and membranes during cellular dehydration. The aim of our study was to assess LEA genes’ expression levels in hydrated (HL) and desiccated leaves (DL) and to identify, characterise, and estimate the potential role of R. serbica LEAPs in desiccation tolerance. In total, 318 LEAPs from HL and DL were identified and classified into the seven LEA protein family groups ranging from LEA1-LEA5, seed maturation proteins (SMPs), and dehydrins (DEH). Analysis of the physicochemical properties, motif architecture, secondary structure, homology, and phylogenetic relationships demonstrated that R. serbica LEAPs greatly differed among the LEA family groups. The most abundant LEA2 proteins (mostly downregulated upon desiccation) exhibited lower hydrophilicity and propensity to fold into organised globular domains. Oppositely, hydrophilic LEA4 proteins tended to form amphipathic, A-type, α-helices. Most of desiccation-upregulated LEA genes encoded highly disordered DEH1, LEA1, LEA4.2, and LEA4.3 proteins. While dehydrins might chelate metals and bind DNA under water deficit, other ID LEAPs (e.g. LEA1, LEA3, LEA4) might participate in forming intracellular proteinaceous condensates or adopt amphipathic α-helical conformation, enabling them to stabilise desiccation-sensitive proteins and membranes. Taken together, possible functions of LEAPs are discussed with significant implications on drought tolerance improvement of crops grown in arid areas.
PB  - Serbian Plant Physiology Society
PB  - Institute for Biological Research “Siniša Stanković” – National Institute of Republic of Serbia, University of Belgrade
PB  - Faculty of Biology, University of Belgrade
C3  - Book of Abstracts / 4th International Conference on Plant Biology [and] 23rd SPPS Meeting, 6-8 October 2022, Belgrade, 2022, 83-
T1  - Late embryogenesis abundant (LEA) proteins in Ramonda serbica Panc identification, classification and structural characterization
SP  - 95
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_3085
ER  - 

@conference{
author = "Pantelic, Ana and Stevanovic, Strahinja and Milić, Dejana and Milić Komić, Sonja and Kilibarda, Nataša and Vidović, Marija",
year = "2022",
abstract = "An ancient resurrection plant Ramonda serbica Panc. is able to survive a long desiccation period and reestablish metabolic activity upon watering. A hallmark of desiccation tolerance in the resurrection species is the accumulation of protective late embryogenesis abundant proteins (LEAPs). These intrinsically disordered proteins (IDPs) may stabilize the correct structure of proteins and membranes during cellular dehydration. The aim of our study was to assess LEA genes’ expression levels in hydrated (HL) and desiccated leaves (DL) and to identify, characterise, and estimate the potential role of R. serbica LEAPs in desiccation tolerance. In total, 318 LEAPs from HL and DL were identified and classified into the seven LEA protein family groups ranging from LEA1-LEA5, seed maturation proteins (SMPs), and dehydrins (DEH). Analysis of the physicochemical properties, motif architecture, secondary structure, homology, and phylogenetic relationships demonstrated that R. serbica LEAPs greatly differed among the LEA family groups. The most abundant LEA2 proteins (mostly downregulated upon desiccation) exhibited lower hydrophilicity and propensity to fold into organised globular domains. Oppositely, hydrophilic LEA4 proteins tended to form amphipathic, A-type, α-helices. Most of desiccation-upregulated LEA genes encoded highly disordered DEH1, LEA1, LEA4.2, and LEA4.3 proteins. While dehydrins might chelate metals and bind DNA under water deficit, other ID LEAPs (e.g. LEA1, LEA3, LEA4) might participate in forming intracellular proteinaceous condensates or adopt amphipathic α-helical conformation, enabling them to stabilise desiccation-sensitive proteins and membranes. Taken together, possible functions of LEAPs are discussed with significant implications on drought tolerance improvement of crops grown in arid areas.",
publisher = "Serbian Plant Physiology Society, Institute for Biological Research “Siniša Stanković” – National Institute of Republic of Serbia, University of Belgrade, Faculty of Biology, University of Belgrade",
journal = "Book of Abstracts / 4th International Conference on Plant Biology [and] 23rd SPPS Meeting, 6-8 October 2022, Belgrade, 2022, 83-",
title = "Late embryogenesis abundant (LEA) proteins in Ramonda serbica Panc identification, classification and structural characterization",
pages = "95",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_3085"
}

Pantelic, A., Stevanovic, S., Milić, D., Milić Komić, S., Kilibarda, N.,& Vidović, M.. (2022). Late embryogenesis abundant (LEA) proteins in Ramonda serbica Panc identification, classification and structural characterization. in Book of Abstracts / 4th International Conference on Plant Biology [and] 23rd SPPS Meeting, 6-8 October 2022, Belgrade, 2022, 83-
Serbian Plant Physiology Society., 95.
https://hdl.handle.net/21.15107/rcub_rimsi_3085

Pantelic A, Stevanovic S, Milić D, Milić Komić S, Kilibarda N, Vidović M. Late embryogenesis abundant (LEA) proteins in Ramonda serbica Panc identification, classification and structural characterization. in Book of Abstracts / 4th International Conference on Plant Biology [and] 23rd SPPS Meeting, 6-8 October 2022, Belgrade, 2022, 83-. 2022;:95.
https://hdl.handle.net/21.15107/rcub_rimsi_3085 .

Pantelic, Ana, Stevanovic, Strahinja, Milić, Dejana, Milić Komić, Sonja, Kilibarda, Nataša, Vidović, Marija, "Late embryogenesis abundant (LEA) proteins in Ramonda serbica Panc identification, classification and structural characterization" in Book of Abstracts / 4th International Conference on Plant Biology [and] 23rd SPPS Meeting, 6-8 October 2022, Belgrade, 2022, 83- (2022):95,
https://hdl.handle.net/21.15107/rcub_rimsi_3085 .

TY  - CONF
AU  - Markovic, Nemanja
AU  - Milić Komić, Sonja
AU  - Radosavljevic, Jelena
AU  - Pantelic, Ana
AU  - Kilibarda, Nataša
AU  - Vidović, Marija
PY  - 2021
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/3084
AB  - Late embryogenesis abundant (LEA) proteins are induced in cellular dehydration, such as freezing, drought, or desiccation. They can be involved in antioxidative defense, ion sequestration, and structural stabilization of both membranes and enzymes during freezing or drying, while by forming intracellular proteinaceous condensates they increase structural integrity and intracellular viscosity of cells during desiccation 1. The genome of the model plant Arabidopsis thaliana contains 51 genes encoding LEA proteins2. The majority of these LEA proteins (35%) belongs to Pfam LEA_4 (PF02987) family. In silico analysis suggested that these proteins are highly hydrophilic proteins with significant intrinsically disordered protein (IDP) properties. In order to evaluate structural properties and possible functions of LEA_4 protein family under different water content, a representative AtLEA25 protein (At2g42560, 635 aa), naturally located in the cytoplasm of seeds3 was obtained in Escherichia coli by recombinant DNA technology. Although this technology has been traditionally used to over-express and purify various globular proteins, numerous reports have shown that the IDPs, due to their structural plasicity are naturally highly susceptible to proteolytic cleavage. To conduct structural and functional studies we developed a robust method to produce highly purified (>95% pure) AtLEA25 with no detectable amount of protein breakdown products.
PB  - Belgrade : Serbian Biochemical Society
C3  - Biochemical Insights into Molecular Mechanisms, 2021, 117-
T1  - Efficient production of highly purified Late Embryogenesis Abundant (LEA) protein from Arabidopsis thaliana by recombinant DNA technology
EP  - 99
SP  - 98
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_3084
ER  - 

@conference{
author = "Markovic, Nemanja and Milić Komić, Sonja and Radosavljevic, Jelena and Pantelic, Ana and Kilibarda, Nataša and Vidović, Marija",
year = "2021",
abstract = "Late embryogenesis abundant (LEA) proteins are induced in cellular dehydration, such as freezing, drought, or desiccation. They can be involved in antioxidative defense, ion sequestration, and structural stabilization of both membranes and enzymes during freezing or drying, while by forming intracellular proteinaceous condensates they increase structural integrity and intracellular viscosity of cells during desiccation 1. The genome of the model plant Arabidopsis thaliana contains 51 genes encoding LEA proteins2. The majority of these LEA proteins (35%) belongs to Pfam LEA_4 (PF02987) family. In silico analysis suggested that these proteins are highly hydrophilic proteins with significant intrinsically disordered protein (IDP) properties. In order to evaluate structural properties and possible functions of LEA_4 protein family under different water content, a representative AtLEA25 protein (At2g42560, 635 aa), naturally located in the cytoplasm of seeds3 was obtained in Escherichia coli by recombinant DNA technology. Although this technology has been traditionally used to over-express and purify various globular proteins, numerous reports have shown that the IDPs, due to their structural plasicity are naturally highly susceptible to proteolytic cleavage. To conduct structural and functional studies we developed a robust method to produce highly purified (>95% pure) AtLEA25 with no detectable amount of protein breakdown products.",
publisher = "Belgrade : Serbian Biochemical Society",
journal = "Biochemical Insights into Molecular Mechanisms, 2021, 117-",
title = "Efficient production of highly purified Late Embryogenesis Abundant (LEA) protein from Arabidopsis thaliana by recombinant DNA technology",
pages = "99-98",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_3084"
}

Markovic, N., Milić Komić, S., Radosavljevic, J., Pantelic, A., Kilibarda, N.,& Vidović, M.. (2021). Efficient production of highly purified Late Embryogenesis Abundant (LEA) protein from Arabidopsis thaliana by recombinant DNA technology. in Biochemical Insights into Molecular Mechanisms, 2021, 117-
Belgrade : Serbian Biochemical Society., 98-99.
https://hdl.handle.net/21.15107/rcub_rimsi_3084

Markovic N, Milić Komić S, Radosavljevic J, Pantelic A, Kilibarda N, Vidović M. Efficient production of highly purified Late Embryogenesis Abundant (LEA) protein from Arabidopsis thaliana by recombinant DNA technology. in Biochemical Insights into Molecular Mechanisms, 2021, 117-. 2021;:98-99.
https://hdl.handle.net/21.15107/rcub_rimsi_3084 .

Markovic, Nemanja, Milić Komić, Sonja, Radosavljevic, Jelena, Pantelic, Ana, Kilibarda, Nataša, Vidović, Marija, "Efficient production of highly purified Late Embryogenesis Abundant (LEA) protein from Arabidopsis thaliana by recombinant DNA technology" in Biochemical Insights into Molecular Mechanisms, 2021, 117- (2021):98-99,
https://hdl.handle.net/21.15107/rcub_rimsi_3084 .

TY  - CONF
AU  - Pantelic, Ana
AU  - Stevanovic, Strahinja
AU  - Kilibarda, Nataša
AU  - Milić Komić, Sonja
AU  - Radosavljevic, Jelena
AU  - Vidović, Marija
PY  - 2021
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/3083
AB  - Endemic plant species, Ramonda serbica is a resurrection plant that can tolerate extreme dehydration (desiccation, loss of 95% of cellular water) even over months. The accumulation of late embryogenesis abundant proteins (LEAPs) is a crucial step in the mechanism of desiccation tolerance. The role of LEAPs is not completely resolved, but they are accepted as intrinsically disordered proteins (IDPs). Based on previously established de novo transcriptome database of R. serbica leaves we identify around 160 members of LEA gene family. Identified LEAPs were classified into six groups: LEA 1-5 and seed maturation proteins (SMPs) according to protein family (Pfam) database. Based on multiple sequence alignment, secondary structure prediction and 3D structure modeling, we conducted LEA protein structure analysis. We showed that more than 50% of identified LEAPs exhibited a high propensity to form α-helices. As predicted by several bioinformatic tools, more than 70% of identified LEAPs were found to be highly disordered. Thus, these proteins are predicted to be disordered in solution, but they acquire a secondary, predominantly α-helical structure during drying, in contrast to globular proteins, which most often causes the loss of structure upon dehydration. By using molecular dynamic simulations, we identified the most favorable conformations of representative LEAPs and we have studied conformational transitions driven by the water scarcity. Structural characterization of LEAPs is a key to understand their function and regulation of their intrinsic structural disorder-to-order transition during desiccation as a requirement for biological function, in order to promote development of new therapeutic strategies in neurodegenerative disorders, cell preservation technology and the improvement of crop drought tolerance.
PB  - Belgrade : Serbian Biochemical Society
C3  - Biochemical Insights into Molecular Mechanisms, 2021, 117-
T1  - Characterization of the late embryogenesis abundant (LEA) proteins family in hydrated and desiccated Ramonda serbica Panc. leaves
EP  - 118
SP  - 117
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_3083
ER  - 

@conference{
author = "Pantelic, Ana and Stevanovic, Strahinja and Kilibarda, Nataša and Milić Komić, Sonja and Radosavljevic, Jelena and Vidović, Marija",
year = "2021",
abstract = "Endemic plant species, Ramonda serbica is a resurrection plant that can tolerate extreme dehydration (desiccation, loss of 95% of cellular water) even over months. The accumulation of late embryogenesis abundant proteins (LEAPs) is a crucial step in the mechanism of desiccation tolerance. The role of LEAPs is not completely resolved, but they are accepted as intrinsically disordered proteins (IDPs). Based on previously established de novo transcriptome database of R. serbica leaves we identify around 160 members of LEA gene family. Identified LEAPs were classified into six groups: LEA 1-5 and seed maturation proteins (SMPs) according to protein family (Pfam) database. Based on multiple sequence alignment, secondary structure prediction and 3D structure modeling, we conducted LEA protein structure analysis. We showed that more than 50% of identified LEAPs exhibited a high propensity to form α-helices. As predicted by several bioinformatic tools, more than 70% of identified LEAPs were found to be highly disordered. Thus, these proteins are predicted to be disordered in solution, but they acquire a secondary, predominantly α-helical structure during drying, in contrast to globular proteins, which most often causes the loss of structure upon dehydration. By using molecular dynamic simulations, we identified the most favorable conformations of representative LEAPs and we have studied conformational transitions driven by the water scarcity. Structural characterization of LEAPs is a key to understand their function and regulation of their intrinsic structural disorder-to-order transition during desiccation as a requirement for biological function, in order to promote development of new therapeutic strategies in neurodegenerative disorders, cell preservation technology and the improvement of crop drought tolerance.",
publisher = "Belgrade : Serbian Biochemical Society",
journal = "Biochemical Insights into Molecular Mechanisms, 2021, 117-",
title = "Characterization of the late embryogenesis abundant (LEA) proteins family in hydrated and desiccated Ramonda serbica Panc. leaves",
pages = "118-117",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_3083"
}

Pantelic, A., Stevanovic, S., Kilibarda, N., Milić Komić, S., Radosavljevic, J.,& Vidović, M.. (2021). Characterization of the late embryogenesis abundant (LEA) proteins family in hydrated and desiccated Ramonda serbica Panc. leaves. in Biochemical Insights into Molecular Mechanisms, 2021, 117-
Belgrade : Serbian Biochemical Society., 117-118.
https://hdl.handle.net/21.15107/rcub_rimsi_3083

Pantelic A, Stevanovic S, Kilibarda N, Milić Komić S, Radosavljevic J, Vidović M. Characterization of the late embryogenesis abundant (LEA) proteins family in hydrated and desiccated Ramonda serbica Panc. leaves. in Biochemical Insights into Molecular Mechanisms, 2021, 117-. 2021;:117-118.
https://hdl.handle.net/21.15107/rcub_rimsi_3083 .

Pantelic, Ana, Stevanovic, Strahinja, Kilibarda, Nataša, Milić Komić, Sonja, Radosavljevic, Jelena, Vidović, Marija, "Characterization of the late embryogenesis abundant (LEA) proteins family in hydrated and desiccated Ramonda serbica Panc. leaves" in Biochemical Insights into Molecular Mechanisms, 2021, 117- (2021):117-118,
https://hdl.handle.net/21.15107/rcub_rimsi_3083 .

TY  - CHAP
AU  - Vidović, Marija
AU  - Milić Komić, Sonja
PY  - 2021
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/2928
AB  - Proteolysis represents a primary recycling system for amino acids. Moreover, by controlling the protein turnover, proteolysis plays an important role in key cellular processes such as control of cell cycle, programmed cell death (including senescence) and response to various stimuli. In eukaryotic cells, most proteins are degraded by autophagy and 26S proteasome machinery, composed in general of 20S proteolytic core and 19S regulatory particle. The protein susceptibility to proteolysis is determined by its structural features. Folded globular proteins in their native state are rarely degraded, however when misfolded, denatured or when an unstructured region is attached, the degradation is promoted. Proteins natively containing intrinsically disordered regions (IDRs) or completely lacking the stable secondary and tertiary structures are defined as intrinsically disordered proteins (IDPs). Due to their high intramolecular flexibility and plasticity, IDPs are involved in DNA metabolism, transcriptional activation, autophagy, and signalling cascades related to response to various stimuli. In sessile organisms such as plants, IDPs enable prompt acclimation to external factors, including light perception, adaptation to oxidative stress and water loss, and regulation of protective, antioxidative and secondary metabolism. Binding of specific ligands and partners to particular IDP triggers structural changes and affects the stability of IDP, its susceptibility to proteolysis and aggregation-propensity. Theabnormal aggregation of several IDPs and altered proteolysis pathways are closely connected with serious neurodegenerative disorders, such as Alzheimer’s and Parkinson's diseases. In this chapter, we discuss the current understanding of proteolytic processes of specific, well-characterised IDPs under different physiological states, emphasizing the influence of the microenvironment and ligands/partners on their conformation.
T2  - A closer look at proteolysis
T1  - Regulation of proteolysis of intrinsically disordered proteins: physiological consequences
EP  - 156
SP  - 111
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_2928
ER  - 

@inbook{
author = "Vidović, Marija and Milić Komić, Sonja",
year = "2021",
abstract = "Proteolysis represents a primary recycling system for amino acids. Moreover, by controlling the protein turnover, proteolysis plays an important role in key cellular processes such as control of cell cycle, programmed cell death (including senescence) and response to various stimuli. In eukaryotic cells, most proteins are degraded by autophagy and 26S proteasome machinery, composed in general of 20S proteolytic core and 19S regulatory particle. The protein susceptibility to proteolysis is determined by its structural features. Folded globular proteins in their native state are rarely degraded, however when misfolded, denatured or when an unstructured region is attached, the degradation is promoted. Proteins natively containing intrinsically disordered regions (IDRs) or completely lacking the stable secondary and tertiary structures are defined as intrinsically disordered proteins (IDPs). Due to their high intramolecular flexibility and plasticity, IDPs are involved in DNA metabolism, transcriptional activation, autophagy, and signalling cascades related to response to various stimuli. In sessile organisms such as plants, IDPs enable prompt acclimation to external factors, including light perception, adaptation to oxidative stress and water loss, and regulation of protective, antioxidative and secondary metabolism. Binding of specific ligands and partners to particular IDP triggers structural changes and affects the stability of IDP, its susceptibility to proteolysis and aggregation-propensity. Theabnormal aggregation of several IDPs and altered proteolysis pathways are closely connected with serious neurodegenerative disorders, such as Alzheimer’s and Parkinson's diseases. In this chapter, we discuss the current understanding of proteolytic processes of specific, well-characterised IDPs under different physiological states, emphasizing the influence of the microenvironment and ligands/partners on their conformation.",
journal = "A closer look at proteolysis",
booktitle = "Regulation of proteolysis of intrinsically disordered proteins: physiological consequences",
pages = "156-111",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_2928"
}

Vidović, M.,& Milić Komić, S.. (2021). Regulation of proteolysis of intrinsically disordered proteins: physiological consequences. in A closer look at proteolysis, 111-156.
https://hdl.handle.net/21.15107/rcub_rimsi_2928

Vidović M, Milić Komić S. Regulation of proteolysis of intrinsically disordered proteins: physiological consequences. in A closer look at proteolysis. 2021;:111-156.
https://hdl.handle.net/21.15107/rcub_rimsi_2928 .

Vidović, Marija, Milić Komić, Sonja, "Regulation of proteolysis of intrinsically disordered proteins: physiological consequences" in A closer look at proteolysis (2021):111-156,
https://hdl.handle.net/21.15107/rcub_rimsi_2928 .