蛋白质导入线粒体过程中两个热休克蛋白70复合物的顺序作用。
Sequential action of two hsp70 complexes during protein import into mitochondria.
作者信息
Horst M, Oppliger W, Rospert S, Schönfeld H J, Schatz G, Azem A
机构信息
Biozentrum, Universität Basel, Switzerland.
出版信息
EMBO J. 1997 Apr 15;16(8):1842-9. doi: 10.1093/emboj/16.8.1842.
Abstract
The mitochondrial chaperone mhsp70 mediates protein transport across the inner membrane and protein folding in the matrix. These two reactions are effected by two different mhsp70 complexes. The ADP conformation of mhsp70 favors formation of a complex on the inner membrane; this 'import complex' contains mhsp70, its membrane anchor Tim44 and the nucleotide exchange factor mGrpE. The ATP conformation of mhsp70 favors formation of a complex in the matrix; this 'folding complex' contains mhsp70, the mitochondrial DnaJ homolog Mdj1 and mGrpE. A precursor protein entering the matrix interacts first with the import complex and then with the folding complex. A chaperone can thus function as part of two different complexes within the same organelle.
摘要
线粒体伴侣蛋白mhsp70介导蛋白质穿过内膜的转运以及基质中的蛋白质折叠。这两个反应由两种不同的mhsp70复合物介导。mhsp70的ADP构象有利于在内膜上形成复合物；这种“输入复合物”包含mhsp70、其膜锚定蛋白Tim44和核苷酸交换因子mGrpE。mhsp70的ATP构象有利于在基质中形成复合物；这种“折叠复合物”包含mhsp70、线粒体DnaJ同源物Mdj1和mGrpE。进入基质的前体蛋白首先与输入复合物相互作用，然后与折叠复合物相互作用。因此，一种伴侣蛋白可以作为同一细胞器内两种不同复合物的一部分发挥作用。
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