Escherichia coli signal recognition particle receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix
Escherichia coli signal recognition particle receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix
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DOI：
10.1074/jbc.m705430200
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发表时间：
2007-11-02
影响因子：
4.8
通讯作者：
Sinning, Irmgard
中科院分区：
文献类型：
--
作者：
Parlitz, Richard;Eitan, Asa;Sinning, Irmgard
大肠杆菌膜蛋白的生物合成是由信号识别颗粒及其膜相关受体（FtsY）介导的。尽管FtsY对它的功能至关重要，但它如何与膜相互作用仍不清楚。严重截断的活性（NG + 1）和非活性（NG）突变体的FtsY之间的结构/功能差异的分析，使我们能够确定一个重要的膜相互作用的决定因素。突变体的三维结构的比较，结合定点诱变，建模，和脂质体结合试验，发现FtsY包含一个保守的自主脂质结合的两亲性α-螺旋在N-末端的N域。删除实验表明，这种螺旋是必不可少的FtsY在体内的功能，从而提供了，第一次，明确的证据，功能上重要的，生理相关的相互作用的FtsY与脂质。
Escherichia coli membrane protein biogenesis is mediated by a signal recognition particle and its membrane-associated receptor ( FtsY). Although crucial for its function, it is still not clear how FtsY interacts with the membrane. Analysis of the structure/function differences between severely truncated active ( NG + 1) and inactive ( NG) mutants of FtsY enabled us to identify an essential membrane-interacting determinant. Comparison of the three-dimensional structures of the mutants, combined with site-directed mutagenesis, modeling, and liposome-binding assays, revealed that FtsY contains a conserved autonomous lipid-binding amphipathic alpha-helix at the N-terminal end of the N domain. Deletion experiments showed that this helix is essential for FtsY function in vivo, thus offering, for the first time, clear evidence for the functionally important, physiologically relevant interaction of FtsY with lipids.