1. Alternative conformations of a group 4 Late Embryogenesis Abundant protein associated to its in vitro protective activity.
- Author
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Rendón-Luna DF, Arroyo-Mosso IA, De Luna-Valenciano H, Campos F, Segovia L, Saab-Rincón G, Cuevas-Velazquez CL, Reyes JL, and Covarrubias AA
- Subjects
- Plant Proteins metabolism, Water metabolism, Embryonic Development, Arabidopsis Proteins genetics, Arabidopsis Proteins metabolism, Arabidopsis metabolism
- Abstract
Late Embryogenesis Abundant (LEA) proteins are a group of intrinsically disordered proteins implicated in plant responses to water deficit. In vitro studies revealed that LEA proteins protect reporter enzymes from inactivation during low water availability. Group 4 LEA proteins constitute a conserved protein family, displaying in vitro protective capabilities. Under water deficiency or macromolecular crowding, the N-terminal of these proteins adopts an alpha-helix conformation. This region has been identified as responsible for the protein in vitro protective activity. This study investigates whether the attainment of alpha-helix conformation and/or particular amino acid residues are required for the in vitro protective activity. The LEA4-5 protein from Arabidopsis thaliana was used to generate mutant proteins. The mutations altered conserved residues, deleted specific conserved regions, or introduced prolines to hinder alpha-helix formation. The results indicate that conserved residues are not essential for LEA4-5 protective function. Interestingly, the C-terminal region was found to contribute to this function. Moreover, alpha-helix conformation is necessary for the protective activity only when the C-terminal region is deleted. Overall, LEA4-5 shows the ability to adopt alternative functional conformations under the tested conditions. These findings shed light on the in vitro mechanisms by which LEA proteins protect against water deficit stress., (© 2024. The Author(s).)
- Published
- 2024
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