Tim54p connects inner membrane assembly and proteolytic pathways in the mitochondrion.

Tim54p connects inner membrane assembly and proteolytic pathways in the mitochondrion.
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DOI:
10.1083/jcb.200706195
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发表时间:
2007-09-24
期刊:
The Journal of cell biology
影响因子:
--
通讯作者:
Koehler CM
Koehler CM
中科院分区:
其他
文献类型:
--
作者:
Hwang DK;Claypool SM;Leuenberger D;Tienson HL;Koehler CM

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Tim 54 p是内膜TIM 22复合物的一种组分,不直接介导内膜底物的输入,但对于300-kD TIM 22复合物的组装/稳定性是必需的。此外,Δ tim 54酵母表现出一种小阴性表型(在F1 Fo ATP酶、ADP/ATP载体、线粒体形态组分或i-AAA蛋白酶Yme 1 p中携带突变的酵母中也观察到)。有趣的是,在我们的菌株背景中的其他输入突变体不是小阴性的。我们报告,Tim 54 p是不参与维护线粒体DNA或线粒体形态。相反,Tim 54 p介导的活动Yme 1 p复合物的装配后,Yme 1 p是通过TIM 23途径进口。缺陷的Yme 1 p组装可能是缺乏功能性Tim 54 p的菌株中的Pete阴性的主要促成因素。因此,Tim 54 p具有两个独立的功能:TIM 22膜复合物的支架/稳定性和Yme 1 p组装成蛋白水解活性复合物。因此,Tim 54 p连接蛋白质的输入,组装和周转途径在细胞内。
Tim54p, a component of the inner membrane TIM22 complex, does not directly mediate the import of inner membrane substrates but is required for assembly/stability of the 300-kD TIM22 complex. In addition, Δtim54 yeast exhibit a petite-negative phenotype (also observed in yeast harboring mutations in the F1Fo ATPase, the ADP/ATP carrier, mitochondrial morphology components, or the i–AAA protease, Yme1p). Interestingly, other import mutants in our strain background are not petite-negative. We report that Tim54p is not involved in maintenance of mitochondrial DNA or mitochondrial morphology. Rather, Tim54p mediates assembly of an active Yme1p complex, after Yme1p is imported via the TIM23 pathway. Defective Yme1p assembly is likely the major contributing factor for the petite-negativity in strains lacking functional Tim54p. Thus, Tim54p has two independent functions: scaffolding/stability for the TIM22 membrane complex and assembly of Yme1p into a proteolytically active complex. As such, Tim54p links protein import, assembly, and turnover pathways in the mitochondrion.
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