| Budget Amount *help |
¥18,590,000 (Direct Cost: ¥14,300,000、Indirect Cost: ¥4,290,000)
Fiscal Year 2014: ¥3,380,000 (Direct Cost: ¥2,600,000、Indirect Cost: ¥780,000)
Fiscal Year 2013: ¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2012: ¥9,880,000 (Direct Cost: ¥7,600,000、Indirect Cost: ¥2,280,000)
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| Outline of Final Research Achievements |
In this study, we revealed that FliJ of bacterial flagella motor is possibly an origin of the rotor in rotary ATPase/synthase such as V- or F-ATPases. Actually, FliJ shows a rotor like function in A3B3 based on both biochemical and structural analysis. This strongly suggests that the rotor domains of the rotary ATPases and the flagellar export apparatus share a common evolutionary origin. Domain-swapped chimeric V1 consisting of both T. thermophilus and E. hirae enzymes were generated. Analysis for these enzymes indicated that the interaction between the nucleotide binding and C-terminal domains of the catalytic A subunit critical in reduction of the ADP inhibition. Based on the reconstituted experiments, we proposed a model in which the relationship between V1-DF and Vo-C corresponds to that between a slotted screwdriver and a head of slotted screw, consistent with our previous result in which the central rotor apparatus is not the major factor for the association of V1 with Vo.
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