In vivo protein-interaction mapping of a mitochondrial translocator protein Tom22 at work
In vivo protein-interaction mapping of a mitochondrial translocator protein Tom22 at work
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DOI：
10.1073/pnas.1105921108
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发表时间：
2011-09-13
影响因子：
11.1
通讯作者：
Endo, Toshiya
中科院分区：
文献类型：
--
作者：
Shiota, Takuya;Mabuchi, Hide;Endo, Toshiya
线粒体蛋白质的输入需要线粒体内外膜上的转运子的协同作用。在这里，我们分析的Tom22，外膜转运TOM40复合物的多功能亚基，与其他转运亚基，如Tom20，Tom40，和Tim50和基板前体蛋白的氨基酸残基的空间分辨率在体内和organello位点特异性光交联的相互作用。由过量的底物前体蛋白或前序列肽引起的交联模式的变化表明Tom22的胞质受体结构域如何接受底物蛋白，以及Tom22的膜间空间结构域如何将它们转移到内膜转运蛋白的Tim50。
Mitochondrial protein import requires cooperation of the machineries called translocators in the outer and inner mitochondrial membranes. Here we analyze the interactions of Tom22, a multifunctional subunit of the outer membrane translocator TOM40 complex, with other translocator subunits such as Tom20, Tom40, and Tim50 and with substrate precursor proteins at a spatial resolution of the amino acid residue by in vivo and in organello site-specific photocross-linking. Changes in cross-linking patterns caused by excess substrate precursor proteins or presequence peptides indicate how the cytosolic receptor domain of Tom22 accepts substrate proteins and how the intermembrane space domain of Tom22 transfers them to Tim50 of the inner-membrane translocator.