Cartwright P, Beilharz T, Hansen P, Garrett J, Lithgow T
School of Biochemistry, La Trobe University, Bundoora 3083, Australia.
J Biol Chem. 1997 Feb 21;272(8):5320-5. doi: 10.1074/jbc.272.8.5320.
We have identified a novel protein, Mft52, in the cytosol of yeast cells. Mft52 has a two-domain structure that includes a receptor-like carboxyl-terminal "acid-bristle" domain, which binds basic, amphipathic mitochondrial targeting sequences. Native Mft52, purified from the cytosol of yeast cells, is found as a large particle eluting in the void volume of a Superose 6 gel filtration column. Fusion proteins, consisting of mitochondrial targeting sequences fused to nonmitochondrial passenger proteins, are targeted to mitochondria in wild-type yeast cells, but defects in the gene encoding Mft52 drastically reduce the delivery of these proteins to the mitochondria. We propose that Mft52 is a subunit of a particle that is part of a system of targeting factors and molecular chaperones mediating the earliest stages of protein targeting to the mitochondria.
我们在酵母细胞的胞质溶胶中鉴定出一种新型蛋白质Mft52。Mft52具有双结构域结构,其中包括一个受体样羧基末端“酸刷毛”结构域,该结构域可结合碱性两亲性线粒体靶向序列。从酵母细胞胞质溶胶中纯化得到的天然Mft52,以大颗粒形式存在,在Superose 6凝胶过滤柱的空体积中洗脱。由与非线粒体乘客蛋白融合的线粒体靶向序列组成的融合蛋白,在野生型酵母细胞中靶向线粒体,但编码Mft52的基因缺陷会大大减少这些蛋白向线粒体的递送。我们提出,Mft52是一种颗粒的亚基,该颗粒是靶向因子和分子伴侣系统的一部分,介导蛋白质靶向线粒体的最早阶段。