Zia Muliani, Dwi Hilda Putri, Yuni Ahda, Syamsurizal, Rikno Harmoko
The Protein disulfide isomerase (PDI), a member of the thioredoxin (TRX) superfamily, is known to mediate the folding of the newly synthesized protein in the endoplasmic reticulum (ER) by catalyzing the formation of thioldisulfide bonds of a polypeptide. PDI also plays as a chaperon by assisting protein re-folding from a denatured state caused by environmental stresses. In the present study, we cloned a cDNA encoding PDI from the soybean seedling (Glycine max L. Merrill cv. Argomulyo), named GmPDI1. Sequencing analysis shows that the open reading frame of GmPDI1 is composed of 1,494 nucleotides, encoding a protein of 500 amino acids. The amino acid sequence of GmPDI1 has a similarity of 85.4% and 86.2% to PDI1 from Arabidopsis thaliana and Arabidopsis lyrata, respectively. Domain structure analysis identified that GmPDI1 has two thioredoxin-like domains, a and a’, containing the di-cysteine motif (CXXC). The GmPDI1 is attributed with 29 aa of signal peptide at N-terminal and ER-retention signal KDEL at C-terminal, indicating that GmPDI1 is localized in the endoplasmic reticulum. © 2023 American Institute of Physics Inc.. All rights reserved.
Department of Biology, Faculty of Mathematics and Natural Science, Universitas Negeri Padang, West Sumatera, Padang, Indonesia; Research Center for Genetic Engineering, Research Organization for Life Sciences and Environment, National Research and Innovation Agency (BRIN), Jl. Raya Jakarta-Bogor, Cibinong, West Java, Bogor, Indonesia
