Kuhn A
Department of Applied Microbiology, University of Karlsruhe, Germany.
FEMS Microbiol Rev. 1995 Aug;17(1-2):185-90. doi: 10.1111/j.1574-6976.1995.tb00201.x.
The membrane insertion of bacteriophage coat proteins occurs independent of the Sec-translocase of Escherichia coli. Detailed study of the Pf3 and M13 coat proteins has elucidated two fundamental mechanisms of how proteins invade the membrane, most likely by direct interaction with the lipid bilayer. The Sec-independent translocation of amino-terminal regions across the inner membrane is limited to a short length and a small number of charged residues. Protein regions that contain several charged residues are efficiently translocated across the membrane when these regions are flanked by two adjacent hydrophobic segments interacting synergistically. The relevance of these findings for the membrane insertion mechanism of multispanning membrane proteins is discussed.
噬菌体外壳蛋白的膜插入过程独立于大肠杆菌的Sec转运酶。对Pf3和M13外壳蛋白的详细研究阐明了蛋白质侵入膜的两种基本机制，很可能是通过与脂质双层的直接相互作用。氨基末端区域跨内膜的Sec非依赖性转运仅限于较短长度和少量带电荷残基。当包含几个带电荷残基的蛋白质区域两侧有两个协同相互作用的相邻疏水片段时，这些区域能有效地跨膜转运。文中讨论了这些发现与多跨膜蛋白膜插入机制的相关性。
