骆驼穿过针眼：Clp ATP 酶的蛋白质解折叠活性
A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases.
作者信息
Zolkiewski Michal
机构信息
Department of Biochemistry, Kansas State University, Manhattan, KS 66506, USA.
出版信息
Mol Microbiol. 2006 Sep;61(5):1094-100. doi: 10.1111/j.1365-2958.2006.05309.x.
Abstract
Clp ATPases are protein machines involved in protein degradation and disaggregation. The common structural feature of Clp ATPases is the formation of ring-shaped oligomers. Recent work has shown that the function of all Clp ATPases is based on an energy-dependent threading of substrates through the narrow pore at the centre of the ring. This review gives an outline of known mechanistic principles of threading machines that unfold protein substrates either before their degradation (ClpA, ClpX, HslU) or during their reactivation from aggregates (ClpB). The place of Clp ATPases within a broad AAA+ superfamily of ATPases associated with various cellular activities suggests that similar mechanisms can be used by other protein machines to induce conformational rearrangements in a wide variety of substrates.
摘要
Clp ATP酶是参与蛋白质降解和解聚的蛋白质机器。Clp ATP酶的共同结构特征是形成环状寡聚体。最近的研究表明，所有Clp ATP酶的功能都基于底物通过环中心狭窄孔道的能量依赖性穿入。本综述概述了已知的穿入机器的机制原理，这些机器在蛋白质底物降解之前（ClpA、ClpX、HslU）或从聚集体中重新激活期间（ClpB）展开蛋白质底物。Clp ATP酶在与各种细胞活动相关的广泛的AAA+ATP酶超家族中的位置表明，其他蛋白质机器可以使用类似的机制在多种底物中诱导构象重排。
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