| Project/Area Number |
04680157
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
物質生物化学
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| Research Institution | Shinshu University |
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Principal Investigator |
AOYAMA Toshifumi Shinshu University School of Medicine, Associate Professor, 医学部, 助教授 (50231105)
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| Project Period (FY) |
1992 – 1993
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| Project Status |
Completed (Fiscal Year 1993)
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| Budget Amount *help |
¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1993: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 1992: ¥1,100,000 (Direct Cost: ¥1,100,000)
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| Keywords | acyl-CoA dehydrogenase / acyl-CoA oxidase / PMP70 / vaccinia virus / overexpression / stability in organelle / cDNA-expression / peroxisome / ワクシニアウイルスベクター / ペルオキシソームへの移行 / Zellweger細胞 / 極長鎖脂肪酸アシルCoA脱水素酵素 / mRNAの安定性 |
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| Research Abstract |
cDNA encoding mitochondrial very-long-chain acyl-CoA dehydrogenase was cloned. Amino acid sequence indicated that the enzyme had about 180 amino acids of extra polypeptide at the carboxyl terminal side, when it was compared with the other acyl-CoA dehydrogenases. A series of mutants, deleting about 60 amino acids of polypeptide from carboxyl terminus, were inserted into vaccinia virus to construct recombinant viruses. Expressed protein in rat hepatoma H4 was examined by means of immunoblot analysis. Mutant protein was less stable in mitochondria than mature protein concerning period after the expression. Mutant protein also lost the features of membrane binding and association to form dimer. These results indicate that the extra polypeptide at carboxyl side has unique function to stabilize the protein in mitochondria. Similar results are obtained concerning the extra polypeptide at carboxyl side of peroxisomal acyl-CoA oxidase.
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