Protein disulphide isomerase family in bread wheat (Triticum aestivum L.): protein structure and expression analysis

Abstract

The deduced amino-acid sequences of 17 protein disulphide isomerase (PDI) and PDI-like cDNAs of wheat assigned to nine homoeologous groups were searched for conserved motives by comparison with characterized sequences in different protein databases. The wheat protein sequences encoded by genes of different homoelogous groups showed a high level of structural similarity with the corresponding protein sequences of other species clustering into the same phylogenetic group. The proteins of five groups (I-V) share two thioredoxin-like active domains and show structural similarities with the corresponding proteins of higher eukaryotes, whereas those of the remaining three groups (VI-VIII) contain a single thioredoxin-like active domain. The expression analysis of the nine non-homoeologous wheat genes, which was carried out by quantitative RT-PCR in developing caryopses and in seedlings subjected to temperature stresses, showed their constitutive although highly variable transcription rate. The comprehensive structural and transcriptional characterization of the PDI and PDI-like genes of wheat performed in this study represents a basis for future functional characterization of the PDI gene family in the hexaploid context of bread wheat.

PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly

“…PDI is ubiquitous in organisms. Structural and functional studies of protein disulfide isomerases (PDIs) from various species, including bacteria, wheat, humans, and yeast etc., have been reported after it was identified as an enzyme that facilitates protein folding [ 13 , 22 , 23 , 24 , 25 , 26 , 27 , 28 ]. Meiri et al categorized 51 PDI-like proteins, which contained four types key domains (a, b, c, and Erp29c), into six clusters based on their sequences [ 29 , 30 ].…”