| Project/Area Number |
24570152
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Functional biochemistry
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| Research Institution | Morioka College (2013-2014)
Kyoto University (2012) |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
AKIYAMA Yoshinori 京都大学, ウイルス研究所, 教授 (10192460)
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| Research Collaborator |
DAIMON Yasushi
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2014: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2013: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2012: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
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| Keywords | 細菌細胞表層 / 表層ストレス応答 / σE / 外膜タンパク質 / リポ多糖 / プロテアーゼ / ジスルフィド結合 / 大腸菌 / タンパク質品質管理 / シグマE / BAM複合体 |
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| Outline of Final Research Achievements |
Escherichia coli is equipped with envelope stress-response systems to sense and cope with disorders of outer membrane (OM) constituents. The σE-dependent stress response system is one of the most important for the maintenance of the OM structure and function. Disruption of yfgC, a σE-regulated gene, sensitizes cells to multiple drugs, suggesting that it is involved in maintaining OM integrity. However, the specific function of YfgC remained unclear. We revealed that YfgC promotes assembly of LptD, an OM protein involved in the transport of lipopolysaccharides, which undergoes intramolecular disulfide rearrangement during its biogenesis. YfgC also promoted degradation of incorrectly folded LptD. BepA thus controls the quality of OM proteins by promoting either the biogenesis or elimination of OM proteins, depending on their folding state. Based on these results, we suggested that YfgC should be renamed as BepA (β-barrel assembly-enhancing protease).
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