Role of ATP in mitochondrial protein import. Conformational alteration of a precursor protein can substitute for ATP requirement.
Role of ATP in mitochondrial protein import. Conformational alteration of a precursor protein can substitute for ATP requirement.
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ATP 在线粒体蛋白质输入中的作用。
DOI：
10.1016/s0021-9258(18)68887-8
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发表时间：
1988
期刊：
影响因子：
--
通讯作者：
Walter Neupert
中科院分区：
文献类型：
--
作者：
N. Pfanner;R. Pfaller;Ralf Kleene;Masaki Ito;M. Tropschug;Walter Neupert
The role of nucleoside triphosphates (NTPs) in the import of porin into the mitochondrial outer membrane was investigated with two forms of the porin precursor: the in vitro synthesized biosynthetic precursor (bs-porin) and a water-soluble form of porin (ws-porin) obtained by subjecting the membrane-derived porin to an acid-base treatment (exposure to trichloroacetic acid, followed by alkali and rapid neutralization). The import of ws-porin into mitochondria did not require NTPs, whereas the import of bs-porin required NTPs. In other characteristics, such as binding to a specific receptor protein on the mitochondrial surface, two-step insertion into the outer membrane, and formation of specific membrane channels, ws-porin was indistinguishable from bs-porin. Thus, the acid-base treatment applied in the preparation of ws-porin can substitute for the NTP-requiring step in mitochondrial protein import. We conclude that NTPs are required for unfolding mitochondrial precursor proteins (“translocation competent folding”).
