TAILIEUCHUNG - Báo cáo khoa học: Molecular cloning and characterization of soybean protein disulfide isomerase family proteins with nonclassic active center motifs

Protein disulfide isomerase (PDI) and other PDI family proteins are mem-bers of the thioredoxin superfamily and are thought to play important roles in disulfide bond formation and isomerization in the endoplasmic reticulum (ER). The exact functions of PDI family proteins in plants remain unknown. | ễFEBS Journal Molecular cloning and characterization of soybean protein disulfide isomerase family proteins with nonclassic active center motifs Kensuke Iwasaki1 Shinya Kamauchi1 z Hiroyuki Wadahama1 Masao Ishimoto2 Teruo Kawada1 and Reiko Urade1 1 Division of Food Science and Biotechnology Graduate Schoolof Agriculture Kyoto University Uji Japan 2 NationalAgriculturalResearch Center for Hokkaido Region Sapporo Japan Keywords cotyledon disulfide bond endoplasmic reticulum protein disulfide isomerase soybean 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@ Present address Osaka Bioscience Institute Suita Japan Database The nucleotide sequence data for the cDNA of GmPDIL-3a GmPDIL-3b and genomic GmPDIL-3b are available in the DDBJ EMBL GenBank databases under accession numbers AB189468 AB189469 and AB303863 respectively Received 2 April2009 revised 14 May 2009 accepted 29 May 2009 doi Protein disulfide isomerase PDI and other PDI family proteins are members of the thioredoxin superfamily and are thought to play important roles in disulfide bond formation and isomerization in the endoplasmic reticulum ER . The exact functions of PDI family proteins in plants remain unknown. In this study we cloned two novel PDI family genes from soybean leaf Glycine max L. Merrill cv. Jack . The cDNAs encode proteins of 520 and 523 amino acids and have been denoted GmPDIL-3a and GmP-DIL-3b respectively. GmPDIL-3a and GmPDIL-3b are the first plant ER PDI family proteins reported to contain the nonclassic redox center motif CXXS C and both proteins are ubiquitously expressed in the plant body. However recombinant GmPDIL-3a and GmPDIL-3b did not function as oxidoreductases or as molecular chaperones in vitro although a proportion of each protein formed complexes in both thiol-dependent and thiol-independent ways in the ER. Expression of .

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