| Project/Area Number |
61480124
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
General medical chemistry
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| Research Institution | Department of Biochemistry, Nara Medical University |
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Principal Investigator |
YOSHIHARA Koichiro Department of Biochemistry, Nara Medical University, 生化学医学部, 助教授 (70075042)
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| Co-Investigator(Kenkyū-buntansha) |
KAMIYA Tomoya Department of Biochemistry, Nara Medical University, 生化学医学部, 教授 (50075040)
大橋 康広 奈良県立医大, 生化学医学部, 助手 (40160600)
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| Project Period (FY) |
1986 – 1988
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| Project Status |
Completed (Fiscal Year 1988)
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| Budget Amount *help |
¥6,500,000 (Direct Cost: ¥6,500,000)
Fiscal Year 1988: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1987: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1986: ¥5,000,000 (Direct Cost: ¥5,000,000)
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| Keywords | DNA pol -primase / Primase-stimulating factor / DNA polymerase / Terminal deoxynucleotidyl transferase / Poly(ADP-ribosyl)ation / ポリADP-リボースポリメラーゼ / DNA-ポリメラーゼαプライマーゼ / プライマーゼ活性促進因子 / ポリADP-リボシル化 / ポリADPーリボースポリメラーゼ / DNAポリメラーゼ / プライマーゼ / プライマーゼ促進因子 / Cーキナーゼ / L1210 / NMN / ADPーリボシル化 / DNAポリメラーゼα / 特異的プライマーゼ促進因子 / ヒストンHl / 酵素活性阻害 |
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| Research Abstract |
This project was carried out to clarify the mechanism of the inhibition of DNA pol -primase upon incubation of the enzyme complex in a reconstituted poly(ADP-ribosyl)-ating enzyme system. Our conclusion is that the enzyme complex was inhibited as a result of poly(ADP-ribosyl)ation of either the DNA pol and/or the primase molecules.
During the study, we found that a highly purified DNA pol -primase requires a stimulatory factor for its primase activity; the protein factor (primase-stimulating factor) was purified to near homogeneity and the properties were characterized. The factor markedly decreased the concentration of rXTP required for the primer synthesis by the enzyme complex.
Poly(ADP-ribosyl)ation of other nuclear enzymes was also examined in this study and we proved that DNA polymerase and terminal deoxynucleotidyl transferase are also poly(ADP-ribosyl)ated and inhibited.
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