TY  - CONF
AU  - Marković, Nemanja
AU  - Milić Komić, Sonja
AU  - Radosavljević, Jelena
AU  - Pantelić, Ana
AU  - Kilibarda, Nataša
AU  - Vidović, Marija
PY  - 2021
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1870
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
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_imagine_1870
ER  - 

@conference{
author = "Marković, Nemanja and Milić Komić, Sonja and Radosavljević, Jelena and Pantelić, 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",
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_imagine_1870"
}

Marković, N., Milić Komić, S., Radosavljević, J., Pantelić, 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
Belgrade : Serbian Biochemical Society., 98-99.
https://hdl.handle.net/21.15107/rcub_imagine_1870

Marković N, Milić Komić S, Radosavljević J, Pantelić 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;:98-99.
https://hdl.handle.net/21.15107/rcub_imagine_1870 .

Marković, Nemanja, Milić Komić, Sonja, Radosavljević, Jelena, Pantelić, 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):98-99,
https://hdl.handle.net/21.15107/rcub_imagine_1870 .