Cloning, Characterization and Overexpression of a Gene (pdiA) Encoding Protein Disulfide Isomerase of Aspergillus oryzae
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概要
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We amplified a 1.1-kb fragment of DNA from genomic DNA of Aspergillus oryzae using the polymerasechain reaction (PCR) and primers, the sequences of which correspond to the consensus sequences coding for two thioredoxin domains of protein disulfide isomerase (PDI). A genomic DNA clone of A. oryzae was isolated by hybridization with the amplified DNA fragment. Southern hybridization analysis revealed that the gene encoding PDI (pdiA) was present in a 5.0-kb XhoI region of the A. oryzae chromosome as a single copy.pdiA contains three putative introns and encodes 515 amino acid residues. The deduced amino acid sequence of A. oryzae PDI exhibits a high degree of homology (51%) with Humicola insolens PDI, while it exhibits less than 20% homology with those of yeast, plants, and mammals. The amino acid sequence contains an N-terminal signal peptide-like sequence, the C-terminal putative endoplasmic reticulum (ER) retention signal, HDEL, and two putative active site sequences (WCGHCK) of PDI. When the cloned pdiA was expressed under the control. of the amyB promoter in an A. oryzae transformant, the PDI activity in the microsomal fraction was about 10-fold higher than that in a microsomal fraction of the recipient strain, indicating that the cloned gene encodes functional PDI.
- 社団法人日本生物工学会の論文
- 1996-12-25
著者
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Kitamoto Katsuhiko
Department of Biotechnology, The University of Tokyo
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Yamada Osamu
National Cardiovascular Center
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Kitamoto Katsuhiko
Department Of Biotechnology The University Of Tokyo
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TAKAHASHI Kojiro
National Research Institute of Brewing
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Lee Byung
National Research Institute Of Brewing
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Kitamoto Katsuhiko
Department Of Applied Biological Chemistry And Department Of Applied Biological Engineering Graduate
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Yamada Osamu
National Research Institute Of Brewing
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