Structural properties and enzyme stabilization function of the intrinsically disordered LEA_4 protein TdLEA3 from wheat

Late Embryogenesis Abundant (LEA) proteins are mostly predicted to be intrinsically disordered proteins (IDPs) that are induced under conditions of cellular dehydration. Their functions, however, are largely unexplored and also their structure and interactions with potential target molecules have on...

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Bibliographic Details
Published in:Scientific reports 2019-03, Vol.9 (1), p.3720-3720, Article 3720
Main Authors: Koubaa, Sana, Bremer, Anne, Hincha, Dirk K., Brini, Faiçal
Format: Article
Language:English
Subjects:
631/449/2661/2665
631/45/612/1981
82/80
Amino acid sequence
Amino acids
Circular dichroism
Dehydration
Drying
Embryogenesis
Embryonic growth stage
Enzymes
Fourier transforms
Freeze-thawing
Glycerol
Homology
Humanities and Social Sciences
Inactivation
L-Lactate dehydrogenase
Lactic acid
LEA protein
multidisciplinary
Protein structure
Proteins
Rehydration
Science
Science (multidisciplinary)
Trifluoroethanol
Wheat
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Summary:Late Embryogenesis Abundant (LEA) proteins are mostly predicted to be intrinsically disordered proteins (IDPs) that are induced under conditions of cellular dehydration. Their functions, however, are largely unexplored and also their structure and interactions with potential target molecules have only recently been investigated in a small number of proteins. Here, we have characterized the wheat LEA protein TdLEA3, which has sequence homology with the group of LEA_4 proteins that are characterized by the 11-mer repeat motif TAQAAKEKAXE. TdLEA3 has five repeats of this imperfectly conserved 11-mer amino acid motif. To investigate the structure of the protein, we used circular dichroism (CD) and Fourier-transform infrared (FTIR) spectroscopy. The data show that TdLEA3 was largely disordered under fully hydrated conditions and acquired α-helical structure upon drying and in the presence of trifluoroethanol (TFE). Moreover, the addition of increasing glycerol concentrations to the protein solution induced a progressive gain in α-helix content. Activity assays indicated that TdLEA3 was able to prevent the inactivation of lactate dehydrogenase (LDH) under heat, dehydration-rehydration and freeze-thaw treatments. In addition, TdLEA3 reduced aggregate formation in the enzyme during these treatments.
ISSN:2045-2322
2045-2322
DOI:10.1038/s41598-019-39823-w