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

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Bremer,  A.
Transcript Profiling, Infrastructure Groups and Service Units, Max Planck Institute of Molecular Plant Physiology, Max Planck Society;

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Hincha,  D. K.
Transcript Profiling, Infrastructure Groups and Service Units, Max Planck Institute of Molecular Plant Physiology, Max Planck Society;

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Citation

Koubaa, S., Bremer, A., Hincha, D. K., & Brini, F. (2019). Structural properties and enzyme stabilization function of the intrinsically disordered LEA_4 protein TdLEA3 from wheat. Scientific Reports, 9(1): 3720. doi:10.1038/s41598-019-39823-w.


Cite as: http://hdl.handle.net/21.11116/0000-0003-2198-C
Abstract
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.