| Project/Area Number |
61580222
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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 |
分子遺伝学・分子生理学
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| Research Institution | Kyto University |
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Principal Investigator |
MINAGAWA Teiichi Kyoto University, Professor, 理学部, 教授 (90025247)
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| Project Period (FY) |
1986 – 1987
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| Project Status |
Completed (Fiscal Year 1987)
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| Budget Amount *help |
¥1,500,000 (Direct Cost: ¥1,500,000)
Fiscal Year 1987: ¥400,000 (Direct Cost: ¥400,000)
Fiscal Year 1986: ¥1,100,000 (Direct Cost: ¥1,100,000)
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| Keywords | DNArecombination proteins / DNA recombination apparatus / DNA translocation apparatus / DNA recombination mechanism / DNA packaging / 相同DNA組換え / 相同DNAの組換え機構 / DNA詰込み系 / DNA詰込み因子 |
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| Research Abstract |
During life cycle bacteriophage DNA has two alternative morphology,monomer and multimer. We have intended to understand this change by analyzing the mechanism of recombination and maturation.
1. DNA recombination. We have investigated the function of recombination genes and gene products (gp) of T4 hage by exploring in vivo functions of cloned genes and in vitro reactions of highly purified gene products. GpuvsX hinds to ssDNA and promotes strand pairing to homologous dsDNA. The pairing reaction is highly stimulated by two other recombination gene products. Gp32 eliminates hair pin structure in ssDNA and gpuvsY promotes binding of gpuvsX to the ssDNA-gp32 complex, thus constituting minimum essential components in recombination apparatus. GpuvsW regulates the formation of intracellular ssDNA. Its mutation increases ssDNA abnormally and works recombinogenic.
2. DNA maturation. We have succeeded in constructing an in vitro system, which is composed of only defined highly purified materials and which packages DNA efficiently into protein coat. At the initial step gp19 binds to core structure (dodecamer of gp8) on prohead and gp18 binds to DNA. These two complexes assemble to 50S assembly. ATP is essential at the initial step as allosteric effector and regulates binding of gp19 to gp8 assembly, and at later step ATP hydrolysis couples with DNA translocation. T4 and lambda DNAs are also packaged and cleaved to a unique length close to but not exactly same with T3 DNA. This system must be a good tool to understand the detail mechanism of initiation of DNA packaging , tranlocation and folding of DNA and cleavage of DNA in phage head formation.
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