http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Goo, Tae-Won,Yun, Eun-Young,Kim, Sung-Wan,Park, Kwang-Ho,Hwang, Jae-Sam,Kwon, O-Yu,Kang, Seok-Woo Korean Society of Sericultural Science 2003 International Journal of Industrial Entomology Vol.7 No.2
Protein disulfide isomerase (PDI) found in the endoplasmic reticulum (ER) catalyzes disulfide bond exchange and assists in protein folding of newly synthesized proteins. PDI also functions as a molecular chaperone and has been found to be associated with proteins in the ER. In addition, PDI functions as a subunit of two more complex enzyme systems: the prolyl-4-hydroxylase and the triacylglycerol transfer proteins. A cDNA that encodes protein disulfide isomerase was previously isolated from Bombyx mori (bPDI), in which open reading frame of 494 amino acids contained two PDI-typical thioredoxin active site of WCGHCK and an ER retention signal of the KDEL motif at its C-terminal, and we report its functional characterization here. This putative bPDI cDNA is expressed in insect Sf9 cells as a recombinant proteins using baculovirus expression vector system. The bPDI recombinant proteins are successfully recognized by antirat PDI antibody, and shown to be biologically active in vitro by mediating the oxidative refolding of reduced and scrambled RNase. This suggests that bPDI may play an important role in protein folding mechanism of insects.
Bombyx mori Protein Disulfide Isomerase Enhances the Production of Nuecin, an Antibacterial Protein
Tae Won Goo,Eun Young Yun,Sung Wan Kim,Kwang Ho Choi,Min Uk Kang,O-Yu Kwon,Seok Woo Kang 한국응용곤충학회 2008 한국응용곤충학회 학술대회논문집 Vol.2008 No.05
The insect baculovirus expression vector system (BEVS) is useful for the production of biologically active recombinant proteins. However, the overexpression of foreign proteins in this system often results in misfolded proteins and the formation of protein aggregates. To overcome this limitation, we have developed a versatile baculovirus expression and secretion system using the Bombyx mori protein disulfide isomerase (bPDI) as a fusion partner. bPDI gene fusion improved the secretion and antibacterial activity of recombinant nuecin proteins. Thus, bPDI gene fusion is a useful addition to the BEVS for the large-scale production of bioactive recombinant proteins.
A Bombyx mori Transcription Factor, ATFC Binds Directly to the UPRE of Molecular Chaperones
Goo, Tae-Won,Yun, Eun-Young,Kim, Sung-Wan,Park, Kwang-Ho,Hwang, Jae-Sam,Kwon, O-Yu,Kang, Seok-Woo Korean Society of Sericultural Science 2003 International Journal of Industrial Entomology Vol.7 No.2
Cells respond to an accumulation of unfolded proteins in the endoplasmic reticulum (ER) by increasing transcription of genes encoding molecular chaperones and folding enzymes. The information is transmitted from the ER lumen to the nucleus by intracellular signaling pathway, called the unfolded protein response (UPR). In Saccharomyces cerevisiae, such induction is mediated by the cis-acting unfolded response element (UPRE) which has been thought to be recognized by Hac1p transcription factor. We cloned the ATFC gene showing similarity with Hac1p, and then examined to determine whether ATFC gene product specifically binds to UPRE by electrophoretic mobility shift assays. ATFC gene product displayed appreciable binding ${to ^{32}}P-labelled$ UPRE. Therefore, we concluded that ATFC represents a major component of the putative transcription factor responsible for the UPR leading to the induction of ER-localized stress proteins.