| Project/Area Number |
09276101
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research on Priority Areas (A)
|
| Allocation Type | Single-year Grants |
|---|
| Research Institution | KYOTO UNIVERSITY |
|---|
Principal Investigator |
YOSHIDA Masasuke Chemical Resources Laboratory Tokyo Institute of Technology, Prof., 資源化学研究所, 教授 (90049073)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
GOTO Yuji Osaka Univ. Prof., 蛋白質研究所, 教授 (40153770)
KOHNO Kenji Nara Ist. Sci. Tech. Prof., 遺伝子教育センター, 教授 (50142005)
KUWAJIMA Kunihiro Tokyo Univ. Prof., 大学院・理学系研究科, 教授 (70091444)
FUNATSU Takashi Waseda Univ. Prof., 理工学部, 助教授 (00190124)
TOKUDA Gen Tokyo Univ. Prof., 分子細胞生物学研究所, 教授 (40125943)
南 康文 大分医科大学, 医学部, 助教授 (40181953)
河田 康志 鳥取大学, 工学部, 助教授 (40177697)
石川 統 東京大学, 大学院・理学系研究科, 教授 (70012482)
|
|---|
| Project Period (FY) |
1997 – 2001
|
| Project Status |
Completed (Fiscal Year 2001)
|
| Budget Amount *help |
¥296,000,000 (Direct Cost: ¥296,000,000)
Fiscal Year 2000: ¥69,000,000 (Direct Cost: ¥69,000,000)
Fiscal Year 1999: ¥79,000,000 (Direct Cost: ¥79,000,000)
Fiscal Year 1998: ¥61,000,000 (Direct Cost: ¥61,000,000)
Fiscal Year 1997: ¥87,000,000 (Direct Cost: ¥87,000,000)
|
|---|
| Keywords | Molecular chaperone, / folding, / stress, / stress protein, / heat-shock protein, / chaperonin, / protein secretion, / purion / 熱ショックタンパク質 / GroEL / 蛋白質の膜透過 / タンパク質 / Hsp90 / タンパク質の膜透過 / インクルージョンボディ |
|---|
| Research Abstract |
Summary
Chaperonin encapsulates unfolded proteins in the cis cavity and ensures safe folding without fear of aggregation. This process requires the energy of ATP hydrolysis. Currently prevailing model of chaperonin function assumes only a single rate-limiting step in whole catalytic cycle of chaperonin, that is, ATP hydrolysis that needs 8 sec. However, Yoshida and Funatsu〓s group have proposed that there are two rate limiting steps in the cycle, one 3 sec and the other 5 sec. This is based on the single molecule observation that GroES release, ADP release, and protein folding initiated by addition of ATP only start after a 3-sec lag phase. Kuwajima showed the conformational change occurred by the ATP binding rather than ATP hydrolysis. Tokuda〓 group have found a new factor, SecG, in SecA system. Similar to SecA, during protein translocation, SecG tumbles in the membrane. Kohno identified that ER stress sensor protein, IRE1-beta, is an RNase that cleaves 28SrRNA. Gotoh succeeded in expression of human beta-microglobulin in yeast cells and pointed out that disulfide bond is important in formation of amyloid fibers. Yoshida〓s group has established a real-time observation system that allows the growth of single amyloid fiber. The result showed that fiber grew predominantly unnidirectionally.
|
