| Budget Amount *help |
¥2,400,000 (Direct Cost: ¥2,400,000)
Fiscal Year 1997: ¥400,000 (Direct Cost: ¥400,000)
Fiscal Year 1996: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1995: ¥1,300,000 (Direct Cost: ¥1,300,000)
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| Research Abstract |
1. A new type of in vitro recombination system was developed on reconstituted chromatin by Drosophila embryos extracts. The reconstituted chromatin templates allow homologous pairing but prevent strand transfer process. These data suggested that the chromatin structure provide genome stability through suppression of aberrant of recombination and that unknown factor (s), remodelling of chromatin structure and/or recombination enzyme complex, would be required for facilitating strand transfer process on chromatin.
2. DMR protein, Drosophila homolog of RecA,has been purified. The protein exhibited DNA binding, ATPase and DNA renaturation activities. DMR protein existed though whole developmental stages, relatively rich in early embryos as well as ovaries. In embryos extract, DMR protein behaves as complex, involving proteins relating on DNA repair and cell cycle. These data suggested that DMR protein would be involved in early embryonic cell proliferation as well as meiotic recombination and that recombination protein complex would be involved in network of nuclear function in higer eucaryotic organism.
DQ1cDNA,Drosophila homolog of RecQ,has been cloned, the amino acid sequence of which was novel and homologous to RecQ in seven helicase motifs. However, an unique C-terminal and short N-terminal stretch of DQ1 was distinct from known higher eucaryotic RecQ homologs. The DQ1 protein was expressed through out the developmental stages with the relatively high level in ovaries and embryos. Therefore, it was suggested that DQ1, a new member of RecQ subfamily, is involved in meiotic recombination and early development.
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