Multiple SecA molecules drive protein translocation across a single translocon with SecG inversion
Multiple SecA molecules drive protein translocation across a single translocon with SecG inversion
复制标题
多个 SecA 分子通过 SecG 反转驱动蛋白质易位跨单个易位子
DOI:
10.1074/jbc.m111.301754
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发表时间:
2012
期刊:
影响因子:
--
通讯作者:
K.
中科院分区:
文献类型:
--
作者:
Morita;K.;Tokuda;H. and Nishiyama;K.
SecA is a translocation ATPase that drives protein translocation. D209N SecA, a dominant-negative mutant, binds ATP but is unable to hydrolyze it. This mutant was inactive to proOmpA translocation. However, it generated a translocation intermediate of 18 kDa. Further addition of wild-type SecA caused its translocation into either mature OmpA or another intermediate of 28 kDa that can be translocated into mature by a proton motive force. The addition of excess D209N SecA during translocation caused a topology inversion of SecG. Moreover, an intermediate of SecG inversion was identified when wild-type and D209N SecA were used in the same amounts. These results indicate that multiple SecA molecules drive translocation across a single translocon with SecG inversion. Here, we propose a revised model of proOmpA translocation in which a single catalytic cycle of SecA causes translocation of 10–13 kDa with ATP binding and hydrolysis, and SecG inversion is required when the next SecA cycle begins with additional ATP hydrolysis.