2013 Fiscal Year Final Research Report
In vitro reconstitution of Type III secretion system - basic and applied research -
| 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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| Keywords | 病原性 / 3型分泌システム / タンパク質大量発現 |
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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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[Journal Article] SptP_<106-136> plays a role in the complex formation with SptP-specific chaperone SicP
Author(s)
Hayashi, F., Kawashima, Y., Takeuchi, S., Okimori, L., Inobe, E., and Oosawa, K.
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Journal Title
Biosci. Biotechnol. Biochem
Volume: (In press)
Peer Reviewed
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