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

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

SUBMITTER: Koubaa S 

PROVIDER: S-EPMC6403280 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature