Mechanism of substrate recognition by bacterial lipoprotein transport equipment
| Project/Area Number |
22780062
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Applied microbiology
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| Research Institution | Kyoto University (2011)
The University of Tokyo (2010) |
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Principal Investigator |
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| Research Collaborator |
TOKUDA Hajime 盛岡大学, 栄養科学部, 教授 (40125943)
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| Project Period (FY) |
2010 – 2011
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| Project Status |
Completed (Fiscal Year 2011)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2011: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2010: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | 細菌細胞表層 / ABCトランスポーター / 細菌 / 蛋白質 / リポ蛋白質 / トランスポーター / 細胞表層 |
|---|
| Research Abstract |
Bacterial lipoproteins represent a subset of membrane-associated proteins that are covalently modified with lipids at the N-terminal cysteine. The final step of lipoprotein modification, N-acylation of apolipoproteins, is mediated by Lnt. lnt null strains could be constructed when LolCDE was overproduced in strains lacking either the major outer membrane lipoprotein Lpp or transpeptidases that cross-link Lpp with peptidoglycan. We revealed that affinity of LolCDE for apolipoprotein is very low, and therefore overexpression of LolCDE is required for its release and sorting to the outer membrane.
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Report
(3 results)
Research Products
(26 results)
