| Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2014: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2013: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2012: ¥3,380,000 (Direct Cost: ¥2,600,000、Indirect Cost: ¥780,000)
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| Outline of Final Research Achievements |
Many bacteria swim by reversibly rotating flagella. The switch complex consists of three switch proteins, FliG, FliM and FliN which control counter clockwise-clockwise (CCW/CW) switching of the motor rotation, form the C-ring on the cytoplasmic face of the MS ring. CheY is a response regulator in bacterial chemotaxis, and phosphorylated CheY (CheY-p) binds to FliM and changes the rotational direction from CCW to CW. We report the C ring structures locked in CCW (che deletion strain) and CW (FliG ΔPAA strain). Comparison of the two strucures showed differences in the position of the C ring and the subunit arrangement in its outer wall. FliM and FliN were well fitted into the middle and lower parts of the outer ring of the C-ring, but the location of FliG remains uncertain. We report the FliG labelling experiments and the structure analysis of the CheY-p bound C ring by electron cryomicroscopy.
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