Binding of SecA ATPase monomers and dimers to lipid vesicles.
Binding of SecA ATPase monomers and dimers to lipid vesicles.
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SecA ATP酶单体和二聚体与脂质囊泡的结合。
DOI：
10.1016/j.bbamem.2019.183112
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发表时间：
2020
期刊：
影响因子：
--
通讯作者：
White,StephenH
中科院分区：
文献类型：
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作者：
Roussel,Guillaume;White,StephenH
大肠杆菌SecA ATP酶马达蛋白对于通过SecYEG转座子将蛋白质分泌到周质空间中是必需的。其功能依赖于与周围脂质双层以及SecYEG易位子的相互作用。带负电荷的脂质是双层结合所必需的，这一点已经知道了超过25年，但几乎没有系统的定量数据。我们已经进行了广泛的调查SecA分配到大单层囊泡（LUV）使用广泛的脂质和电解质组合物，包括主要的细胞质盐的大肠杆菌。我们已经证明谷氨酸钾可以稳定SecA。对于典型的E，水到双层的转移自由能约为-7.5 kcalmol-1。胶体脂质组合物。虽然已经确定SecA在细胞质中是二聚体，但我们发现最广泛引用的二聚体形式（PDB 1 M6 N）仅弗罗姆. colilipids。
TheEscherichia coliSecA ATPase motor protein is essential for secretion of proteins through the SecYEG translocon into the periplasmic space. Its function relies upon interactions with the surrounding lipid bilayer as well as SecYEG translocon. That negatively charged lipids are required for bilayer binding has been known for >25 years, but little systematic quantitative data is available. We have carried out an extensive investigation of SecA partitioning into large unilamellar vesicles (LUV) using a wide range of lipid and electrolyte compositions, including the principal cytoplasmic salt ofE. coli, potassium glutamate, which we have shown stabilizes SecA. The water-to-bilayer transfer free energy is about −7.5 kcal mol−1for typicalE. colilipid compositions. Although it has been established that SecA is dimeric in the cytoplasm, we find that the most widely cited dimer form (PDB 1M6N) binds only weakly to LUVs formed fromE. colilipids.