An intersubunit signaling network coordinates ATP hydrolysis by m-AAA proteases.
An intersubunit signaling network coordinates ATP hydrolysis by m-AAA proteases.
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DOI：
10.1016/j.molcel.2009.07.018
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发表时间：
2009-09-11
期刊：
影响因子：
16
通讯作者：
Tatsuta, Takashi
中科院分区：
文献类型：
--
作者：
Augustin, Steffen;Gerdes, Florian;Lee, Sukyeong;Tsai, Francis T. F.;Langer, Thomas;Tatsuta, Takashi
环状AAA+ atp酶通过底物的展开和大分子结构的重塑来控制多种细胞过程。然而，AAA+环内ATP水解是如何被调节并与机械功耦合的，人们知之甚少。在这里，我们证明了m-AAA蛋白酶环复合物内ATP的协同水解，线粒体内膜上保守的AAA+机器。ATP与一个AAA亚基结合抑制邻近亚基的ATP水解，导致AAA环内ATP的协调而非随机水解。无偏遗传筛选确定了涉及保守AAA基序的亚基间信号通路，并揭示了atp酶活性与AAA中心孔环的密切耦合。底物的膜位错需要邻近亚基之间协调的ATP水解，而底物加工则不需要。这些发现为AAA+蛋白如何将ATP水解产生的能量转化为机械功提供了新的见解。
Ring-shaped AAA+ ATPases control a variety of cellular processes by substrate unfolding and remodeling of macromolecular structures. However, how ATP hydrolysis within AAA+ rings is regulated and coupled to mechanical work is poorly understood. Here, we demonstrate coordinated ATP hydrolysis within m-AAA protease ring complexes, conserved AAA+ machines in the inner membrane of mitochondria. ATP binding to one AAA subunit inhibits ATP hydrolysis by the neighboring subunit leading to coordinated rather than stochastic ATP hydrolysis within the AAA ring. Unbiased genetic screens define an intersubunit signaling pathway involving conserved AAA motifs and reveal an intimate coupling of ATPase activities to central AAA pore loops. Coordinated ATP hydrolysis between adjacent subunits is required for membrane dislocation of substrates but not for substrate processing. These findings provide new insight how AAA+ proteins convert energy derived from ATP hydrolysis into mechanical work.
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