Assembly of the mitochondrial membrane system. 3. Function and synthesis of the oligomycin sensitivity-conferring protein of yeast mitochondria.
Assembly of the mitochondrial membrane system. 3. Function and synthesis of the oligomycin sensitivity-conferring protein of yeast mitochondria.
复制标题
线粒体膜系统的组装。
DOI：
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发表时间：
1970
影响因子：
4.8
通讯作者：
A. Tzagoloff
中科院分区：
文献类型：
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作者：
A. Tzagoloff
摘要从酵母线粒体中分离纯化了一种与牛心肌线粒体寡霉素敏感性相关蛋白（OSCP）性质相同的蛋白。该蛋白刺激F1与提取膜的结合高达10倍。重组颗粒ATP酶被鲁塔霉素抑制。酵母OSCP本身不与F1形成复合物，在没有膜的情况下也不赋予F1对鲁塔霉素的敏感性。OSCP的功能似乎与F1与存在于膜中的ATP酶的另一组分的结合密切相关。在氯霉素存在下，低浓度葡萄糖解阻遏的酵母细胞的核糖体后上清液已被证明含有可溶性OSCP。存在于细胞质组分中的OSCP的量足以结合也存在于该组分中的所有可溶性F1。结论：OSCP和F1均由细胞质-核糖体系统合成。
Abstract A protein with the same properties as the oligomycin sensitivity-conferring protein (OSCP) of bovine heart mitochondria has been purified from yeast mitochondria. This protein stimulates the binding of F1 to extracted membranes by as much as 10-fold. The reconstituted particulate ATPase is inhibited by rutamycin. The yeast OSCP by itself does not form a complex with F1 nor does it confer rutamycin sensitivity on F1 in the absence of the membrane. The function of OSCP appears to be closely related to the binding of F1 to another component of the ATPase which is present in the membrane. The postribosomal supernatant of yeast cells derepressed on low concentrations of glucose in the presence of chloramphenicol has been shown to contain soluble OSCP. The amount of OSCP present in the cytoplasmic fraction is sufficient to bind all of the soluble F1 also present in this fraction. It is concluded that both OSCP and F1 are synthesized by the cytoplasmic-ribosomal system of the cell.