| Project/Area Number |
23790468
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Bacteriology (including Mycology)
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| Research Institution | Gunma University |
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Principal Investigator |
HAYASHI Fumio 群馬大学, 理工学研究院, 助教 (60400777)
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| Project Period (FY) |
2011 – 2012
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥3,510,000 (Direct Cost: ¥2,700,000、Indirect Cost: ¥810,000)
Fiscal Year 2012: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2011: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
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| Keywords | 病原性 / 3型分泌システム / タンパク質大量発現 / 再構成 / エフェクター / シャペロン / 3型分泌装置 / 3型分泌 / サルモネラ |
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| Research Abstract |
SptP is a virulence effector protein of Salmonella that is involved in bacterial invasion into a host cell. For effective secretion, SptP forms a complex with SptP-specific chaperone SicP through its chaperone-binding domain, residues 35-139. We suggested that residues 106-136 of SptP are important for complex formation with SicP by in vitro reconstitution experiments. The dissociation of the SptP/SicP complex requires ATPase activity of InvC. So, we purified InvC, and then characterized its ATPase activity and tested whether InvC ATPase dissociates the complex. InvC ATPase activity showed positive cooperativity, suggesting that InvC subunits form a homo-oligomer. Furthermore the ATPase activity was stimulated in the presence of liposomes, suggesting that InvC interacts with plasma membrane and the activity is regulated by the interaction. In the presence of liposomes and SptP/SicP complexes, InvC ATPase activity was not increased further and did not dissociate SptP/SicP complexes.
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