Folding and biogenesis of mitochondrial small Tim proteins.
Folding and biogenesis of mitochondrial small Tim proteins.
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DOI：
10.3390/ijms140816685
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发表时间：
2013-08-13
影响因子：
5.6
通讯作者：
Lu H
中科院分区：
文献类型：
--
作者：
Ceh-Pavia E;Spiller MP;Lu H
正确的折叠对所有蛋白质的功能至关重要主要集中于调节氧化还原状态在IMS中，配置的半胱氨酸保留：氧化折叠至关重要，但是氧化（二硫键）蛋白质不能将其进口到线粒体中。这些蛋白质。组装（MIA）途径既催化tim蛋白质的氧化，又是小蛋白的氧化折叠，这是一个由静电和疏水相互作用的多步骤的过程。 Ursors胞质溶胶，其进口，氧化折叠，复杂的组装和IMS功能。
Correct and timely folding is critical to the function of all proteins. The importance of this is illustrated in the biogenesis of the mitochondrial intermembrane space (IMS) “small Tim” proteins. Biogenesis of the small Tim proteins is regulated by dedicated systems or pathways, beginning with synthesis in the cytosol and ending with assembly of individually folded proteins into functional complexes in the mitochondrial IMS. The process is mostly centered on regulating the redox states of the conserved cysteine residues: oxidative folding is crucial for protein function in the IMS, but oxidized (disulfide bonded) proteins cannot be imported into mitochondria. How the redox-sensitive small Tim precursor proteins are maintained in a reduced, import-competent form in the cytosol is not well understood. Recent studies suggest that zinc and the cytosolic thioredoxin system play a role in the biogenesis of these proteins. In the IMS, the mitochondrial import and assembly (MIA) pathway catalyzes both import into the IMS and oxidative folding of the small Tim proteins. Finally, assembly of the small Tim complexes is a multistep process driven by electrostatic and hydrophobic interactions; however, the chaperone function of the complex might require destabilization of these interactions to accommodate the substrate. Here, we review how folding of the small Tim proteins is regulated during their biogenesis, from maintenance of the unfolded precursors in the cytosol, to their import, oxidative folding, complex assembly and function in the IMS.
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