The C-tail anchored TssL subunit, an essential protein of the enteroaggregative Escherichia coli Sci-1 Type VI secretion system, is inserted by YidC.

The C-tail anchored TssL subunit, an essential protein of the enteroaggregative Escherichia coli Sci-1 Type VI secretion system, is inserted by YidC.
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DOI:
10.1002/mbo3.9
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发表时间:
2012-03
期刊:
影响因子:
3.4
通讯作者:
Cascales, Eric
Cascales, Eric
中科院分区:
生物学3区
文献类型:
--
作者:
Aschtgen, Marie-Stephanie;Zoued, Abdelrahim;Lloubes, Roland;Journet, Laure;Cascales, Eric

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VI 型分泌系统(T6SS)是革兰氏阴性细菌中存在的大分子复合物。 T6SS 在结构上与噬菌体细胞穿刺装置相似,并且已被证明可以介导细菌与宿主或细菌与细菌之间的相互作用。 T6SS 组装 13 至 20 种蛋白质。在肠聚集性大肠杆菌 (EAEC) 中,其中一个亚组件由形成跨包膜复合物的四种蛋白质组成:TssJ 外膜脂蛋白、肽聚糖锚定的内膜 TagL 蛋白以及两种假定的内膜蛋白 TssL 和 TssM。在本研究中,我们从定位、拓扑和功能方面表征了 EAEC Sci-1 T6SS 的 TssL 蛋白。 TssL 是 T6SS 的关键组成部分,通过位于蛋白质 C 末端的单个跨膜片段锚定到内膜上。我们进一步表明,该跨膜片段对于蛋白质的功能至关重要,其在内膜中的正确插入取决于 YidC 并受到 Hsp70 同源物 DnaK 的调节。
Type VI secretion systems (T6SS) are macromolecular complexes present in Gram-negative bacteria. T6SS are structurally similar to the bacteriophage cell-puncturing device and have been shown to mediate bacteria–host or bacteria–bacteria interactions. T6SS assemble from 13 to 20 proteins. In enteroaggregative Escherichia coli (EAEC), one of the subassemblies is composed of four proteins that form a trans-envelope complex: the TssJ outer membrane lipoprotein, the peptidoglycan-anchored inner membrane TagL protein, and two putative inner membrane proteins, TssL and TssM. In this study, we characterized the TssL protein of the EAEC Sci-1 T6SS in terms of localization, topology, and function. TssL is a critical component of the T6SS, anchored to the inner membrane through a single transmembrane segment located at the extreme C-terminus of the protein. We further show that this transmembrane segment is essential for the function of the protein and its proper insertion in the inner membrane is dependent upon YidC and modulated by the Hsp70 homologue DnaK.
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