Membrane localization and topology of the Yersinia pestis YscJ lipoprotein.
Membrane localization and topology of the Yersinia pestis YscJ lipoprotein.
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DOI：
10.1099/mic.0.2007/013045-0
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发表时间：
2008-02
期刊：
影响因子：
1.5
通讯作者：
E. Silva-Herzog;Franco Ferracci;Michael W. Jackson;Sabrina S. Joseph;G. Plano
中科院分区：
文献类型：
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作者：
E. Silva-Herzog;Franco Ferracci;Michael W. Jackson;Sabrina S. Joseph;G. Plano
研究了鼠疫耶尔森菌III型分泌器官的重要组成部分YscJ脂蛋白的定位和膜拓扑结构。YscJ被证明是一种内膜（IM）脂蛋白，通过n端脂质片段和c端跨膜（TM）结构域锚定在IM的质周表面。无论在+2或+3位置发现的氨基酸残基如何，n端脂质片段都会定位到IM。IM定位依赖于完整的n端结构域（氨基酸+1至+61），表明该区域在YscJ定位中起作用。相比之下，IM定位不需要YscJ c端域和TM域。n端序列分析表明，很大一部分膜定位的YscJ缺乏n -酰化，这是脂蛋白依赖于lo转运到OM所需的最后修饰。有趣的是，YscJ功能需要将n端连接到IM上；然而，YscV蛋白的第一个TM结构域可以在功能上取代YscJ分泌信号和脂盒，这表明与IM的附着机制并不重要。
The localization and membrane topology of the Yersinia pestis YscJ lipoprotein, an essential component of the type III secretion apparatus, was investigated. YscJ was demonstrated to be an inner membrane (IM) lipoprotein that is anchored to the periplasmic face of the IM via an N-terminal lipid moiety and via a C-terminal transmembrane (TM) domain. Localization of the N-terminal lipid moiety to the IM occurred regardless of the amino-acid residues found in the +2 or +3 positions. IM localization was dependent upon an intact N-terminal domain (amino acids +1 to +61), suggesting that this region plays a role in YscJ localization. In contrast, the YscJ C-terminal domain and TM domain were not required for IM localization. N-terminal sequence analysis demonstrated that a significant proportion of membrane-localized YscJ lacks N-acylation, the final modification required for Lol-dependent transport of a lipoprotein to the OM. Interestingly, attachment of the N-terminus to the IM was required for YscJ function; however, the YscJ secretion signal and lipo-box could be functionally replaced by the first TM domain of the YscV protein, suggesting that the mechanism of attachment to the IM was not critical.