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首页> 外文期刊>Journal of bacteriology >Cleavage, methylation, and localization of the Pseudomonas aeruginosa export proteins XcpT, -U, -V, and -W.
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Cleavage, methylation, and localization of the Pseudomonas aeruginosa export proteins XcpT, -U, -V, and -W.

机译：铜绿假单胞菌输出蛋白XcpT，-U，-V和-W的切割，甲基化和定位。

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Four components of the apparatus of extracellular protein secretion of Pseudomonas aeruginosa, Xcpt, -U, -V, and -W (XcpT-W), are synthesized as precursors with short N-terminal leader peptides that share sequence similarity with the pilin subunit of this organism. A specialized leader peptidase/methylase, product of the pilD gene, has been shown to cleave the leader peptide from prepilin and to methylate the N-terminal phenylalanine of the mature pilin. Antibodies were prepared against XcpT-W and used to purify each of these proteins. Sequence analysis of XcpT-W has shown that these proteins, like mature pilin, contain N-methylphenylalanine as the N-terminal amino acid. Analysis of cellular fractions from wild-type and pilD mutant strains of P. aeruginosa showed that the precursor forms of XcpT-W are located predominantly in the bacterial inner membrane, and their localization is not altered after PilD-mediated removal of the leader sequence. These studies demonstrate that the biogenesis of the apparatus of extracellular protein secretion and that of type IV pili share a requirement for PilD. This bifunctional enzyme, acting in the inner membrane, cleaves the leader peptides from precursors of pilins and XcpT-W and subsequently methylates the amino group of the N-terminal phenylalanine of each of its substrates.
机译：合成铜绿假单胞菌细胞外蛋白分泌装置Xcpt，-U，-V和-W（XcpT-W）的四个成分，作为具有短N末端前导肽的前体，这些肽与S的菌毛素亚基共享序列相似性。这种生物。已经显示，pilD基因的产物是一种专门的前导肽酶/甲基化酶，可以从前菌毛蛋白上裂解前导肽，并使成熟菌毛蛋白的N末端苯丙氨酸甲基化。制备了针对XcpT-W的抗体，并用于纯化每种蛋白质。 XcpT-W的序列分析表明，这些蛋白质像成熟的菌毛蛋白一样，含有N-甲基苯基丙氨酸作为N末端氨基酸。对来自铜绿假单胞菌的野生型和pilD突变菌株的细胞级分的分析表明，XcpT-W的前体形式主要位于细菌内膜中，并且在PilD介导的前导序列去除后，其定位没有改变。这些研究表明，细胞外蛋白分泌装置的生物发生与IV型菌毛的生物发生共享PilD的需求。这种作用在内膜上的双功能酶从纤毛蛋白和XcpT-W的前体上裂解前导肽，然后甲基化其每个底物N末端苯丙氨酸的氨基。

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