Microtubule disassembly by ATP-dependent oligomerization of the AAA enzyme katanin
Microtubule disassembly by ATP-dependent oligomerization of the AAA enzyme katanin
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DOI：
10.1126/science.286.5440.782
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发表时间：
1999-10-22
期刊：
影响因子：
56.9
通讯作者：
Vale, RD
中科院分区：
文献类型：
--
作者：
Hartman, JJ;Vale, RD
Katanin是AAA腺苷三磷酸酶（ATPase）超家族的一员，利用核苷酸水解能切断和分解微管。许多AAA酶可分解稳定的蛋白质复合物，但其机制尚不清楚。荧光共振能量转移分析表明，角朊蛋白的p60亚基以三磷酸腺苷（ATP）和微管依赖的方式寡聚。寡聚化增加了katanin对微管的亲和力，刺激了其atp酶活性。在ATP水解后，微管结合的katanin低聚物将微管分解，然后解离成游离的katanin单体。将核苷酸依赖的寡聚化循环耦合到靶蛋白复合物的分解可能是atp水解AAA结构域的一般特征。
Katanin, a member of the AAA adenosine triphosphatase (ATPase) superfamily, uses nucleotide hydrolysis energy to sever and disassemble microtubules. Many AAA enzymes disassemble stable protein-protein complexes, but their mechanisms are not well understood. A fluorescence resonance energy transfer assay demonstrated that the p60 subunit of katanin oligomerized in an adenosine triphosphate (ATP)- and microtubule-dependent manner. Oligomerization increased the affinity of katanin for microtubules and stimulated its ATPase activity. After hydrolysis of ATP, microtubule-bound katanin oligomers disassembled microtubules and then dissociated into free katanin monomers. Coupling a nucleotide-dependent oligomerization cycle to the disassembly of a target protein complex may be a general feature of ATP-hydrolyzing AAA domains.