Grant-in-Aid for Scientific Research on Priority Areas.
|Research Institution||The Tokyo Metropolitan Institute of Medical Science|
YAHARA Ichiro The Tokyo Metropolitan Institute of Medical Science, Vice-Director, 副所長 (60109957)
深沢 俊夫 慶応義塾大学, 医学部, 教授 (90029934)
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)
YOSHIDA Masasuke Tokyo Inst.Tech., Res.Lab.Resources Utilization, Professor, 資源化学研究所, 教授 (90049073)
|Project Fiscal Year
1993 – 1995
Completed(Fiscal Year 1996)
|Budget Amount *help
¥61,200,000 (Direct Cost : ¥61,200,000)
Fiscal Year 1996 : ¥3,000,000 (Direct Cost : ¥3,000,000)
Fiscal Year 1995 : ¥18,000,000 (Direct Cost : ¥18,000,000)
Fiscal Year 1994 : ¥18,000,000 (Direct Cost : ¥18,000,000)
Fiscal Year 1993 : ¥22,200,000 (Direct Cost : ¥22,200,000)
|Keywords||stress response / stress protein / heat shock protein / molecular chaperone / oxidative stress / SOS response / protein folding / intracellular transport of proteins / ストレス応答 / ストレス蛋白質 / 熱ショック蛋白質 / 分子シャペロン / 酸化ストレス / SOS応答 / 蛋白質のフォールディング / 蛋白質の細胞内輸送|
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.