The secretion apparatus of Pseudomonas aeruginosa:: identification of a fifth pseudopilin, XcpX (GspK family)
The secretion apparatus of Pseudomonas aeruginosa:: identification of a fifth pseudopilin, XcpX (GspK family)
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DOI：
10.1046/j.1365-2958.1998.00653.x
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发表时间：
1998-01-01
影响因子：
3.6
通讯作者：
Filloux, A
中科院分区：
文献类型：
--
作者：
Bleves, S;Voulhoux, R;Filloux, A
铜绿假单胞菌中的rep基因产物是跨外膜分泌蛋白质所必需的。四种Xcp蛋白，XcpT、U、V和W，在它们的N-末端呈现与IV型皮利亚基的序列同源性，因此它们被命名为假青霉素。在这项研究中，我们的特点xcpX基因产物，一个双位胞质膜蛋白。值得注意的是，氨基酸序列的比较也表明，XcpX蛋白类似于菌毛蛋白和假菌毛蛋白的N-末端。我们表明，XcpX可以处理的prepilin肽酶，PilD/XcpA，和高度保守的甘氨酸残基前的疏水段不能突变而不损失的XcpX功能。因此，我们将XcpX（GspK）分类为该系统的第五个假阿片肽。
The rep gene products in Pseudomonas aeruginosa are required for the secretion of proteins across the outer membrane. Four of the Xcp proteins, XcpT, U, V and W, present sequence homology to the subunits of type IV pili at their N-termini, and they were therefore designated pseudopilins. In this study, we characterized the xcpX gene product, a bitopic cytoplasmic membrane protein. Remarkably, amino acid sequence comparisons also suggested that the XcpX protein resembles the pilins and pseudopilins at the N-terminus. We show that XcpX could be processed by the prepilin peptidase, PilD/XcpA, and that the highly conserved glycine residue preceding the hydrophobic segment could not be mutated without loss of the XcpX function. We, therefore, classified XcpX (GspK) as the fifth pseudopilin of the system.