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首页> 外文期刊>The FEBS journal >Dissection of LolB function - lipoprotein binding, membrane targeting and incorporation of lipoproteins into lipid bilayers
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Dissection of LolB function - lipoprotein binding, membrane targeting and incorporation of lipoproteins into lipid bilayers

机译：LolB功能的解剖-脂蛋白结合，膜靶向和脂蛋白掺入脂质双层

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摘要

Escherichia coli cells express at least 90 species of lipoprotein. LolB is one of the essential outer membrane lipoproteins, being involved in the last step of lipoprotein sorting. It accepts lipoproteins from a periplasmic molecular chaperone, LolA, and mediates the outer membrane anchoring of lipoproteins through a largely unknown mechanism. It has been shown previously that a LolB derivative, mLolB, lacking an N-terminal acyl chain, can bind lipoproteins. We examined how the lack of an N-terminal anchor affects the outer membrane anchoring of lipoproteins. Surprisingly, mLolB compensates for LolB function and supports E. coli growth, indicating that the N-terminal anchor is not essential for its function. Indeed, mLolB correctly localizes lipoproteins to either the inner or outer membrane depending on the sorting signal at the steady state. Furthermore, periplasmic mLolB enables the dissection of LolB function, namely lipoprotein binding, membrane targeting and lipoprotein anchoring. It mediates the transfer of lipoproteins from LolA to the outer membrane, but also the inner membrane and liposomes, indicating that mLolB exhibits no membrane preference and targets to phospholipids. Consequently, an outer membrane-specific lipoprotein is transiently mislocalized to the inner membrane when cells express only mLolB. LolB anchored to the outer membrane does not cause such mislocalization and is more active than mLolB. Phosphatidylethanolamine has been found to stimulate the mLolB-dependent membrane anchoring of lipoproteins. Taken together, these results indicate that lipoprotein binding, membrane targeting and membrane incorporation of lipoproteins are intrinsic functions of LolB.
机译：大肠杆菌细胞表达至少90种脂蛋白。 LolB是必需的外膜脂蛋白之一，参与脂蛋白分选的最后一步。它从周质分子伴侣LolA接受脂蛋白，并通过一个未知的机制介导脂蛋白的外膜锚定。先前已经证明，缺少N末端酰基链的LolB衍生物mLolB可以结合脂蛋白。我们检查了缺少N末端锚的方式如何影响脂蛋白的外膜锚固。出人意料的是，mLolB补偿了LolB的功能并支持大肠杆菌的生长，这表明N末端锚对其功能并不是必不可少的。实际上，mLolB可以根据稳态下的分选信号将脂蛋白正确定位在内膜或外膜上。此外，周质mLolB能够解剖LolB功能，即脂蛋白结合，膜靶向和脂蛋白锚定。它介导脂蛋白从LolA转移到外膜，但也转移到内膜和脂质体，表明mLolB没有膜偏好性，并靶向磷脂。因此，当细胞仅表达mLolB时，外膜特异性脂蛋白会暂时错位到内膜。锚定在外膜上的LolB不会引起这种错误定位，并且比mLolB更具活性。已经发现磷脂酰乙醇胺可刺激脂蛋白的mLolB依赖性膜锚定。综上所述，这些结果表明脂蛋白结合，脂蛋白的膜靶向和膜掺入是LolB的固有功能。

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