TAILIEUCHUNG - Báo cáo khoa học: Protein disulfide isomerase family proteins involved in soybean protein biogenesis

Protein disulfide isomerase family proteins are known to play important roles in the folding of nascent polypeptides and the formation of disulfide bonds in the endoplasmic reticulum. In this study, we cloned two similar protein disulfide isomerase family genes from soybean leaf (Glycine maxL. Merrill cv. Jack) mRNA by RT-PCR using forward and reverse primers designed from the expressed sequence tag clone sequences. | ỊFEBS Journal Protein disulfide isomerase family proteins involved in soybean protein biogenesis Hiroyuki Wadahama1 Shinya Kamauchi1 Masao Ishimoto2 Teruo Kawada1 and Reiko Urade1 1 Graduate Schoolof Agriculture Kyoto University Uji Japan 2 NationalAgriculturalResearch Center for Hokkaido Region Sapporo Japan Keywords endoplasmic reticulum protein disulfide isomerase soybean storage protein unfolded protein response Correspondence R. Urade Graduate Schoolof Agriculture Kyoto University Uji Kyoto 611-0011 Japan Fax 81 774 38 3758 Tel 81 774 38 3757 E-mail urade@ Database The nucleotide sequence data for GmPDIS-1 GmPDIS-2 BiP calreticulin and b-conglycinin a are available in the DDBJ EMBL GenBank databases under accession numbers AB182630 AB182631 AB210900 AB196794 and AB113351 These authors contributed equally to this work Received 23 July 2006 revised 5 October 2006 accepted 22 November 2006 doi Protein disulfide isomerase family proteins are known to play important roles in the folding of nascent polypeptides and the formation of disulfide bonds in the endoplasmic reticulum. In this study we cloned two similar protein disulfide isomerase family genes from soybean leaf Glycine max L. Merrill cv. Jack mRNA by RT-PCR using forward and reverse primers designed from the expressed sequence tag clone sequences. The cDNA encodes a protein of either 364 or 362 amino acids named GmPDIS-1 or GmPDIS-2 respectively. The nucleotide and amino acid sequence identities of GmPDIS-1 and GmPDIS-2 were 68 and 74 respectively. Both proteins lack the C-terminal endoplasmic reticulum-retrieval signal KDEL. Recombinant proteins of both GmPDIS-1 and GmPDIS-2 were expressed in Escherichia coli as soluble folded proteins that showed both an oxidative refolding activity of denatured ribonuclease A and a chaperone activity. Their domain structures were identified as containing two thioredoxin-like domains a and a and an ERp29c domain by .

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