Synthetic and Structural Biology Approach for Understanding Mechanism of AAA-ATPase

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We extensively used the 3D structural information of the N-terminal domains which were isolated from the other part of AAA-ATPases (Class I and II). We succeeded in determining the tubulin binding site on Katanin p^60 N-terminal domain. Subsequently we found a novel Ca^2+-dependent regulatory mechanism of Katanin’s ATPase activity. For NVL2, the solution structure as well as binding target of N-terminal domain were determined. We thus proposed two hypothesis, one is for the molecular mechanisms on microtubule severing, and another is for the cellular function of NVL2.We extensively used the 3D structural information of the N-terminal domains which were isolated from the other part of AAA-ATPases (Class I and II). We succeeded in determining the tubulin binding site on Katanin p60 N-terminal domain. Subsequently we found a novel Ca2+-dependent regulatory mechanism of Katanin’s ATPase activity. For NVL2, the solution structure as well as binding target of N-terminal domain were determined. We thus proposed two hypothesis, one is for the molecular mechanisms on microtubule severing, and another is for the cellular function of NVL2.