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首页> 美国卫生研究院文献>Molecular and Cellular Biology >Late-Stage Maturation of the Rieske Fe/S Protein: Mzm1 Stabilizes Rip1 but Does Not Facilitate Its Translocation by the AAA ATPase Bcs1
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Late-Stage Maturation of the Rieske Fe/S Protein: Mzm1 Stabilizes Rip1 but Does Not Facilitate Its Translocation by the AAA ATPase Bcs1

机译：Rieske Fe / S蛋白的后期成熟：Mzm1稳定Rip1但不方便其通过AAA ATPase Bcs1转运。

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摘要

The final step in the assembly of the ubiquinol-cytochrome c reductase or bc1 complex involves the insertion of the Rieske Fe/S cluster protein, Rip1. Maturation of Rip1 occurs within the mitochondrial matrix prior to its translocation across the inner membrane (IM) in a process mediated by the Bcs1 ATPase and subsequent insertion into the bc1 complex. Here we show that the matrix protein Mzm1 functions as a Rip1 chaperone, stabilizing Rip1 prior to the translocation step. In the absence of Mzm1, Rip1 is prone to either proteolytic degradation or temperature-induced aggregation. A series of Rip1 truncations were engineered to probe motifs necessary for Mzm1 interaction and Bcs1-mediated translocation of Rip1. The Mzm1 interaction with Rip1 persists in Rip1 variants lacking its transmembrane domain or containing only its C-terminal globular Fe/S domain. Replacement of the globular domain of Rip1 with that of the heterologous folded protein Grx3 abrogated Mzm1 interaction; however, appending the C-terminal 30 residues of Rip1 to the Rip1-Grx3 chimera restored Mzm1 interaction. The Rip1-Grx3 chimera and a Rip1 truncation containing only the N-terminal 92 residues each induced stabilization of the bc1:cytochrome oxidase supercomplex in a Bcs1-dependent manner. However, the Rip1 variants were not stably associated with the supercomplex. The induced supercomplex stabilization by the Rip1 N terminus was independent of Mzm1.
机译：组装泛醇-细胞色素c还原酶或bc1复合物的最后一步涉及插入Rieske Fe / S簇蛋白Rip1。 Rip1的成熟发生在线粒体基质内，然后在Bcs1 ATPase介导的过程中跨内膜（IM）转运并随后插入bc1复合物中。在这里，我们显示基质蛋白Mzm1充当Rip1分子伴侣，在转位步骤之前稳定Rip1。在没有Mzm1的情况下，Rip1容易发生蛋白水解降解或温度诱导的聚集。工程设计了一系列的Rip1截短序列，以探测Mzm1相互作用和Bcs1介导的Rip1转运所需的基序。与Rip1的Mzm1相互作用在缺少其跨膜结构域或仅包含其C端球状Fe / S结构域的Rip1变体中仍然存在。用异源折叠蛋白Grx3取代Rip1的球状结构域消除了Mzm1的相互作用；但是，将Rip1的C端30个残基附加到Rip1-Grx3嵌合体可恢复Mzm1的相互作用。 Rip1-Grx3嵌合体和仅包含N末端92个残基的Rip1截短均以Bcs1依赖性方式诱导bc1：细胞色素氧化酶超复合物的稳定。但是，Rip1变体与超复合物不稳定。 Rip1 N末端诱导的超复合物稳定独立于Mzm1。

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