De Novo Transcriptome Sequencing of Ramonda serbica Identification of Late Embryogenesis Abundant Proteins
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An extreme loss of cellular water or desiccation (5-10% of relative water content) leads to protein denaturation,
aggregation and degradation, and affects the fluidity of membrane lipids resulting in loss of membrane
integrity [1]. The essential constituents of vegetative desiccation tolerance in so-called resurrection plants
are late embryogenesis abundant proteins (LEAPs). This heterogeneous group of anhydrobiosis-related
intrinsically disordered proteins forms mostly random conformation when fully hydrated, turning into
compact α-helices during desiccation [2]. Based on in vitro studies, LEAPs can be involved in water binding,
ion sequestration, stabilization of both membrane and enzymes during freezing or drying, while by forming
intracellular proteinaceous condensates they increase structural integrity and intracellular viscosity of cells
during desiccation.
Here, we identify 164 members of LEA gene family in endemic and relict resurrection species Ramonda serbica
by int...egrating previously done de novo transcriptome and homologues protein motifs. Identified LEAPs
were classification into six groups according to Protein family (PFAM) database and the most populated
group was LEA4 containing 47% of total identified LEAPs. By using four secondary structure predictors, we
showed that this group exhibited a high propensity to form amphipathic α-helices (81% of total sequence
length is predicted to form α-helical structure). This implies that charged residues might be exposed to the
solvent, while hydrophobic amino acids might interact with lipid bilayers or with other target proteins in
the cell. In addition, as predicted by several bioinformatics tools, more than 70% of identified LEAPs were
found to be highly disordered. Structural characterization of LEAPs is a key to understand their function
and regulation of their intrinsic structural disorder-to-order transition during desiccation. These findings
will promote transformative advancements in various fields, such as the development of new strategies in
neurodegenerative disorders, cell preservation technology and the improvement of crop drought tolerance.
Keywords:
desiccation tolerance / intrinsically disordered proteins / liquid-liquid phase separation / resurrection plants / secondary structure prediction / water stressSource:
Biologia Serbica, 2021, 43, 1 (Special Edition), 65-Publisher:
- Novi Sad : Faculty of Sciences, Department of Biology and Ecology
Funding / projects:
- LEAPSyn-SCI - Late Embryogenesis Abundant Proteins: Structural Characterisation and Interaction With Α-Synuclein (RS-ScienceFundRS-Promis-6039663)
- Ministry of Science, Technological Development and Innovation of the Republic of Serbia, institutional funding - 200042 (University of Belgrade, Institute of Molecular Genetics and Genetic Engineering) (RS-MESTD-inst-2020-200042)
Note:
- Book of Abstracts: Belgrade BioInformatics Conference 2021
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Institut za molekularnu genetiku i genetičko inženjerstvoTY - CONF PY - 2021 UR - https://imagine.imgge.bg.ac.rs/handle/123456789/1877 AB - An extreme loss of cellular water or desiccation (5-10% of relative water content) leads to protein denaturation, aggregation and degradation, and affects the fluidity of membrane lipids resulting in loss of membrane integrity [1]. The essential constituents of vegetative desiccation tolerance in so-called resurrection plants are late embryogenesis abundant proteins (LEAPs). This heterogeneous group of anhydrobiosis-related intrinsically disordered proteins forms mostly random conformation when fully hydrated, turning into compact α-helices during desiccation [2]. Based on in vitro studies, LEAPs can be involved in water binding, ion sequestration, stabilization of both membrane and enzymes during freezing or drying, while by forming intracellular proteinaceous condensates they increase structural integrity and intracellular viscosity of cells during desiccation. Here, we identify 164 members of LEA gene family in endemic and relict resurrection species Ramonda serbica by integrating previously done de novo transcriptome and homologues protein motifs. Identified LEAPs were classification into six groups according to Protein family (PFAM) database and the most populated group was LEA4 containing 47% of total identified LEAPs. By using four secondary structure predictors, we showed that this group exhibited a high propensity to form amphipathic α-helices (81% of total sequence length is predicted to form α-helical structure). This implies that charged residues might be exposed to the solvent, while hydrophobic amino acids might interact with lipid bilayers or with other target proteins in the cell. In addition, as predicted by several bioinformatics tools, more than 70% of identified LEAPs were found to be highly disordered. Structural characterization of LEAPs is a key to understand their function and regulation of their intrinsic structural disorder-to-order transition during desiccation. These findings will promote transformative advancements in various fields, such as the development of new strategies in neurodegenerative disorders, cell preservation technology and the improvement of crop drought tolerance. PB - Novi Sad : Faculty of Sciences, Department of Biology and Ecology C3 - Biologia Serbica T1 - De Novo Transcriptome Sequencing of Ramonda serbica Identification of Late Embryogenesis Abundant Proteins IS - 1 (Special Edition) SP - 65 VL - 43 UR - https://hdl.handle.net/21.15107/rcub_imagine_1877 ER -
@conference{ year = "2021", abstract = "An extreme loss of cellular water or desiccation (5-10% of relative water content) leads to protein denaturation, aggregation and degradation, and affects the fluidity of membrane lipids resulting in loss of membrane integrity [1]. The essential constituents of vegetative desiccation tolerance in so-called resurrection plants are late embryogenesis abundant proteins (LEAPs). This heterogeneous group of anhydrobiosis-related intrinsically disordered proteins forms mostly random conformation when fully hydrated, turning into compact α-helices during desiccation [2]. Based on in vitro studies, LEAPs can be involved in water binding, ion sequestration, stabilization of both membrane and enzymes during freezing or drying, while by forming intracellular proteinaceous condensates they increase structural integrity and intracellular viscosity of cells during desiccation. Here, we identify 164 members of LEA gene family in endemic and relict resurrection species Ramonda serbica by integrating previously done de novo transcriptome and homologues protein motifs. Identified LEAPs were classification into six groups according to Protein family (PFAM) database and the most populated group was LEA4 containing 47% of total identified LEAPs. By using four secondary structure predictors, we showed that this group exhibited a high propensity to form amphipathic α-helices (81% of total sequence length is predicted to form α-helical structure). This implies that charged residues might be exposed to the solvent, while hydrophobic amino acids might interact with lipid bilayers or with other target proteins in the cell. In addition, as predicted by several bioinformatics tools, more than 70% of identified LEAPs were found to be highly disordered. Structural characterization of LEAPs is a key to understand their function and regulation of their intrinsic structural disorder-to-order transition during desiccation. These findings will promote transformative advancements in various fields, such as the development of new strategies in neurodegenerative disorders, cell preservation technology and the improvement of crop drought tolerance.", publisher = "Novi Sad : Faculty of Sciences, Department of Biology and Ecology", journal = "Biologia Serbica", title = "De Novo Transcriptome Sequencing of Ramonda serbica Identification of Late Embryogenesis Abundant Proteins", number = "1 (Special Edition)", pages = "65", volume = "43", url = "https://hdl.handle.net/21.15107/rcub_imagine_1877" }
(2021). De Novo Transcriptome Sequencing of Ramonda serbica Identification of Late Embryogenesis Abundant Proteins. in Biologia Serbica Novi Sad : Faculty of Sciences, Department of Biology and Ecology., 43(1 (Special Edition)), 65. https://hdl.handle.net/21.15107/rcub_imagine_1877
De Novo Transcriptome Sequencing of Ramonda serbica Identification of Late Embryogenesis Abundant Proteins. in Biologia Serbica. 2021;43(1 (Special Edition)):65. https://hdl.handle.net/21.15107/rcub_imagine_1877 .
"De Novo Transcriptome Sequencing of Ramonda serbica Identification of Late Embryogenesis Abundant Proteins" in Biologia Serbica, 43, no. 1 (Special Edition) (2021):65, https://hdl.handle.net/21.15107/rcub_imagine_1877 .