Protein handling by molecular chaperones
Project Area | Protein community: organization and maintenance of protein functions |
Project/Area Number |
19058004
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Research Category |
Grant-in-Aid for Scientific Research on Priority Areas
|
Allocation Type | Single-year Grants |
Review Section |
Biological Sciences
|
Research Institution | Kyoto Sangyo University (2009-2011) Tokyo Institute of Technology (2007-2008) |
Principal Investigator |
|
Co-Investigator(Kenkyū-buntansha) |
WATANABE Yohei 甲南大学, 理工学部, 講師 (40411839)
MOTOJIMA Fumihiro 京都産業大学, 総合生命科学部, 助教 (70372464)
NUREKI Satoshi 東京大学, 理学系研究科, 教授 (10272460)
|
Project Period (FY) |
2007 – 2011
|
Project Status |
Completed (Fiscal Year 2011)
|
Budget Amount *help |
¥109,900,000 (Direct Cost: ¥109,900,000)
Fiscal Year 2011: ¥23,100,000 (Direct Cost: ¥23,100,000)
Fiscal Year 2010: ¥23,100,000 (Direct Cost: ¥23,100,000)
Fiscal Year 2009: ¥23,100,000 (Direct Cost: ¥23,100,000)
Fiscal Year 2008: ¥23,100,000 (Direct Cost: ¥23,100,000)
Fiscal Year 2007: ¥17,500,000 (Direct Cost: ¥17,500,000)
|
Keywords | シャペロン / シャペロニン / GroEL / DnaK / DafA / ClpB / GroES / C1pB / FtsH / プロテアーゼ / おれたたみ / 分子シャペロン |
Research Abstract |
We found two kinds of new membrane chaperones. pspA repairs the leaks of ions through damaged membranes, and uncI assists membrane integration of hydrophobic c-subunit of ATP synthase. DnaK-DnaJ-DafA turns out to be inactive complex. As temperature raises, the complex dissociates and Dnak and DnaJ start to work as disaggregation chaperone in cooperation with ClpB. Polypeptide in the GroEL cage capped by GroES spends most time as tethered state. Then, it is released into the chaperonin cage or outside.
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Report
(7 results)
Research Products
(49 results)