| Co-Investigator(Kenkyū-buntansha) |
YOSHIDA Masasuke Tokyo Inst.Tech., Res.Lab.Resources Utilization, Professor, 資源化学研究所, 教授 (90049073)
ISHIHAMA Akira Nat.Inst.Genetics, Dept.Mol.Genetics, Professor, 分子遺伝, 教授 (80019869)
KAGAWA Yasuo Jichi Med.School, Professor, 医学部, 教授 (30048962)
HORIUCHI Kensuke Nat.Inst.Genetics.Dept.Cell.Genetics.Professor, 細胞遺伝, 教授 (70219210)
NAGATA Kazuhiro Kyoto University, Inst.Chest Diseases, Professor, 胸部疾患研究所, 教授 (50127114)
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| Research Abstract |
1) Molecular chaperone function of HSP90, a major stress protein, has been clarified..
2) Molecular structure of RuvC,an endonuclease induced by the SOS response which recognizes intermediate structures of DNA recombination has been determined by X-ray crystallography. Function of RuvC was also anlyzed.
3) Subunit proteins of 26S and 20S proteasomes have been identified. Their cDNA's have been isolated and their functions have been extensively analyzed.
4) sigma32, a stress-specific transcription factor, has been shown to be quantitatively regulated by stimulation of translation and its stabilization.
5.A new protease, FtsH,been discovered and shown to belong to the AAA family. In addition, FtsH has been shown to degradate sigma32.
6.Functions of the collagen-specific molecular chaperone, HSP47, have been elucidated.
7.A chaperonin specific for insect endosymbiosis (symbionin) has been identified and characterized. In addition, Its cDNA was cloned and its expression was confirmed.
8.Intermediate structures of substrate proteins recognized by chaperonin have been investigated.
9.The mitochondria-transport stimulating factor, MSF,has been newly identified and characterized. Its cDNA has been cloned and its expression was examined with a variety of cell types.
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