| Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2020: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2019: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2018: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Outline of Final Research Achievements |
Outer membrane of gram-negative bacteria contains β-barreled outer membrane proteins. An Escherichia coli periplasmic protein BepA contributes to the maintenance of the structure and quality of the outer membrane by promoting the assembly of outer membrane proteins through its chaperone-like activity, and by degrading and removing abnormal outer membrane proteins through its protease activity. To elucidate the mechanism by which BepA discriminate between outer membrane proteins to be assembled and those to be degraded, we constructed BepA mutants and analyzed their function. We found that the α9/H246 loop located near the protease active site of BepA normally suppresses the protease activity of BepA, and that the reversible conformational change of this loop induces the protease activity of BepA to degrade outer membrane proteins.
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