MOLECULAR-CLONING OF A FUNGAL CDNA-ENCODING PROTEIN DISULFIDE-ISOMERASE

被引：27

作者：

KAJINO, T ^{[1
]}

SARAI, K ^{[1
]}

IMAEDA, T ^{[1
]}

IDEKOBA, C ^{[1
]}

ASAMI, O ^{[1
]}

YAMADA, Y ^{[1
]}

HIRAI, M ^{[1
]}

UDAKA, S ^{[1
]}

机构：

[1] NAGOYA UNIV, FAC AGR, DEPT APPL BIOL SCI, CHIKUSA KU, NAGOYA 464, JAPAN

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1994年 / 58卷 / 08期

关键词：

D O I：

10.1271/bbb.58.1424

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Based on the partial amino acid sequences of a protein disulfide isomerase (PDI) from Humicola insolens, two primers were synthesized for reverse transcriptase mediated ploymerase chain reaction (RT-PCR) of a fungal RNA. A 0.2-kbp fragment around the consensus sequence of PDIs was obtained and used as a probe for screening a fungal cDNA library. A cDNA clone of PDI from H. insolens was isolated and encoded a polypeptide consisting of 505 amino acids, which was characterized by a N-terminal signal sequence composed of 20 amino acids, a consensus sequence (WCGHCK) at two positions, and a C-terminal endoplasmic reticulum retention signal (HDEL). Bacillus brevis harboring an expression plasmid bearing the fungal PDT cDNA was prepared and its culture supernatant showed a significant PDI activity. This indicates that glycosylation of a fungal PDI is not essential for the enzymatic activity related to an interchange of disulfide bonds.

引用

页码：1424 / 1429

页数：6

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