The SecA ATPase motor protein binds to Escherichia coli liposomes only as monomers.,Biochimica et Biophysica Acta (BBA) - Biomembranes

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The SecA ATPase motor protein binds to Escherichia coli liposomes only as monomers.
Biochimica et Biophysica Acta (BBA) - Biomembranes ( IF 2.8 ) Pub Date : 2020-05-13 , DOI: 10.1016/j.bbamem.2020.183358
Guillaume Roussel ₁ , Stephen H White ₁

Affiliation

The essential SecA motor ATPase acts in concert with the SecYEG translocon to secrete proteins into the periplasmic space of Escherichia coli. In aqueous solutions, SecA exists largely as dimers, but the oligomeric state on membranes is less certain. Crystallographic studies have suggested several possible solution dimeric states, but its oligomeric state when bound to membranes directly or indirectly via the translocon is controversial. We have shown using disulfide crosslinking that the principal solution dimer, corresponding to a crystallographic dimer (PDB 1M6N), binds only weakly to large unilamellar vesicles (LUV) formed from E. coli lipids. We report here that other soluble crosslinked crystallographic dimers also bind weakly, if at all, to LUV. Furthermore, using a simple glutaraldehyde crosslinking scheme, we show that SecA is always monomeric when bound to LUV formed from E. coli lipids.

中文翻译：

SecA ATPase 马达蛋白仅作为单体与大肠杆菌脂质体结合。

必需的 SecA 运动 ATPase 与 SecYEG 易位子协同作用，将蛋白质分泌到大肠杆菌的周质空间中。在水溶液中，SecA 主要以二聚体形式存在，但膜上的寡聚状态不太确定。晶体学研究已经提出了几种可能的溶液二聚状态，但是当通过转运子直接或间接与膜结合时，其寡聚状态是有争议的。我们已经使用二硫化物交联表明，对应于结晶二聚体 (PDB 1M6N) 的主要溶液二聚体仅与由大肠杆菌脂质形成的大单层囊泡 (LUV) 弱结合。我们在这里报告其他可溶性交联结晶二聚体也弱结合，如果有的话，LUV。此外，使用简单的戊二醛交联方案，

更新日期：2020-05-19

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