| Project/Area Number |
61480472
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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 |
分子遺伝学・分子生理学
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| Research Institution | University of Tokyo |
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Principal Investigator |
MOGAMI Kaname Research Associate, Fac. of Science, Univ. of Tokyo, 理学部物理学教室, 助手 (80174332)
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| Co-Investigator(Kenkyū-buntansha) |
HOTTA Yoshiki Professor, Fac. of Science, Univ. of Tokyo, 理学部物理学教室, 教授 (30010036)
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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 |
¥6,900,000 (Direct Cost: ¥6,900,000)
Fiscal Year 1988: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1987: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1986: ¥5,400,000 (Direct Cost: ¥5,400,000)
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| Keywords | Drosophila / Muscle mutants / Actin / Myosin / P因子 / ミオシン重鎖 / 単一P因子法 / 筋原繊維 / 形態形成 |
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| Research Abstract |
Indireet flight muscle of the fruit fly Drosophila melanogaster is a set of a large muscle fibers which supply power during flight. Before this project, the head investigator has isolated a number of dominant flightless mutants, and has identified five myosin heavy chain gene mutations. Mutations of a actin gene and a tropomyosin gene have been identified by other investigators. Results of this project were as follows.
1. Non-lethal myosin heavy chain mutations.
Previously reportod myosin heavy chain mutations are homozygous lethal. However, recent research showed that the gene produces many isoforms utilizing a complex process of alternative mRNA splicing. If mutations occurred in a exon specific to the indirect flight muscle, they may be viable. Four mutations were identified as such a mutation. They are genetically inseparable from the lethal alleles, failed to accumulate myosin molecules in the indirect flight muscle, and there are no thick filaments in the muscle.
2. Molecular analysis of actin mutations.
Actin genes of the 3rd chromosomal mutations were cloned and their DNA sequences were investigated. So far, eight mutations were found to have aberrant sequences.
3. Biochemical analysis of mutant actin molecules.
In order to investigate effects of amino acid substitution in actin molecules, mutant molecules were prepared from acetone powder of flies. One mutant actin showed no detectable differences from the normal molecules, the other were not extracted from the powder.
4. A tumor related actin gene.
The normal actin gene was in vitro mutagenized so that it has the same mutation with actin found in a human fibroblast. Flies were transformed with this gene using a transposon P-element. The gene caused deformation of the muscle.
5. A single P-element mutagenisis.
Flightless mutants were isolated using a single P-element insertional mutagenesis method. One hundred and eighty candidates were so far obtained.
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