Channel Formation by Yeast F-ATP Synthase and the Role of Dimerization in the Mitochondrial Permeability Transition
Channel Formation by Yeast F-ATP Synthase and the Role of Dimerization in the Mitochondrial Permeability Transition
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DOI：
10.1074/jbc.c114.559633
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发表时间：
2014-06-06
影响因子：
4.8
通讯作者：
Bernardi, Paolo
中科院分区：
文献类型：
--
作者：
Carraro, Michela;Giorgio, Valentina;Bernardi, Paolo
酵母线粒体的纯化 F-ATP 合酶二聚体表现出 Ca2+ 依赖性通道活性，其特性类似于哺乳动物的通透性转换孔 (PTP)。经过允许电泳 Ca2+ 吸收的 Ca2+ 离子载体 ETH129 处理后，分离的酵母线粒体由于 PTP 打开而经历内膜透化。酵母突变株 Delta TIM11 和 Delta ATP20（分别缺乏二聚体形成所必需的 e 和 g F-ATP 合酶亚基）对 PTP 开放表现出惊人的抵抗力。这些结果表明酵母 PTP 源自 F-ATP 合酶，并表明原位孔形成需要二聚化。
Purified F-ATP synthase dimers of yeast mitochondria display Ca2+ -dependent channel activity with properties resembling those of the permeability transition pore (PTP) of mammals. After treatment with the Ca2+ ionophore ETH129, which allows electrophoretic Ca2+ uptake, isolated yeast mitochondria undergo inner membrane permeabilization due to PTP opening. Yeast mutant strains Delta TIM11 and Delta ATP20 (lacking the e and g F-ATP synthase subunits, respectively, which are necessary for dimer formation) display a striking resistance to PTP opening. These results show that the yeast PTP originates from F-ATP synthase and indicate that dimerization is required for pore formation in situ.