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Type VI secretion and bacteriophage tail tubes share a common assembly pathway.VI 型分泌系统和噬菌体尾管共享一个共同的组装途径。
EMBO Rep. 2014 Mar;15(3):315-21. doi: 10.1002/embr.201337936. Epub 2014 Jan 31.
2
Crystal structure and self-interaction of the type VI secretion tail-tube protein from enteroaggregative Escherichia coli.来自肠聚集性大肠杆菌的VI型分泌尾管蛋白的晶体结构与自身相互作用
PLoS One. 2014 Feb 14;9(2):e86918. doi: 10.1371/journal.pone.0086918. eCollection 2014.
3
Structure-Function Analysis of the C-Terminal Domain of the Type VI Secretion TssB Tail Sheath Subunit.结构功能分析 VI 型分泌系统 TssB 尾部鞘蛋白 C 端结构域。
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Cell Width Dictates Type VI Secretion Tail Length.细胞宽度决定了 VI 型分泌系统的尾部长度。
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Systematic dissection of the agrobacterium type VI secretion system reveals machinery and secreted components for subcomplex formation.系统剖析农杆菌 VI 型分泌系统揭示亚复合物形成的机器和分泌成分。
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Proteogenomic annotation of T6SS components identified in secretome.对分泌蛋白组中鉴定出的VI型分泌系统(T6SS)组分进行蛋白质基因组注释。
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Initiation of H1-T6SS dueling between .启动 H1-T6SS 决斗。
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Qualitative and Quantitative Methods to Measure Antibacterial Activity Resulting from Bacterial Competition.测量细菌竞争产生的抗菌活性的定性和定量方法。
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Microbiol Spectr. 2023 Mar 14;11(2):e0504522. doi: 10.1128/spectrum.05045-22.
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Type VI Secretion Systems: Environmental and Intra-host Competition of Vibrio cholerae.VI 型分泌系统:霍乱弧菌的环境和宿主内竞争。
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Bacterial type VI secretion system (T6SS): an evolved molecular weapon with diverse functionality.细菌VI型分泌系统(T6SS):一种具有多种功能的进化分子武器。
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Label-free relative quantitative proteomics reveals extracellular vesicles as a vehicle for effector protein delivery.无标记相对定量蛋白质组学揭示细胞外囊泡是效应蛋白传递的载体。
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本文引用的文献

1
Crystal structure and self-interaction of the type VI secretion tail-tube protein from enteroaggregative Escherichia coli.来自肠聚集性大肠杆菌的VI型分泌尾管蛋白的晶体结构与自身相互作用
PLoS One. 2014 Feb 14;9(2):e86918. doi: 10.1371/journal.pone.0086918. eCollection 2014.
2
Dissection of the TssB-TssC interface during type VI secretion sheath complex formation.解析 TssB-TssC 界面在 VI 型分泌鞘复合体形成过程中的作用。
PLoS One. 2013 Nov 25;8(11):e81074. doi: 10.1371/journal.pone.0081074. eCollection 2013.
3
Haemolysin coregulated protein is an exported receptor and chaperone of type VI secretion substrates.溶血素调节蛋白是一种分泌型受体和伴侣蛋白,可转运 VI 型分泌系统底物。
Mol Cell. 2013 Sep 12;51(5):584-93. doi: 10.1016/j.molcel.2013.07.025. Epub 2013 Aug 15.
4
PAAR-repeat proteins sharpen and diversify the type VI secretion system spike.PAAR 重复蛋白使 VI 型分泌系统刺突变锋利并多样化。
Nature. 2013 Aug 15;500(7462):350-353. doi: 10.1038/nature12453. Epub 2013 Aug 7.
5
TssK is a trimeric cytoplasmic protein interacting with components of both phage-like and membrane anchoring complexes of the type VI secretion system.TssK 是一种三聚体细胞内蛋白,与噬菌体样和 VI 型分泌系统膜锚定复合物的组成成分相互作用。
J Biol Chem. 2013 Sep 20;288(38):27031-27041. doi: 10.1074/jbc.M113.499772. Epub 2013 Aug 6.
6
Systematic dissection of the agrobacterium type VI secretion system reveals machinery and secreted components for subcomplex formation.系统剖析农杆菌 VI 型分泌系统揭示亚复合物形成的机器和分泌成分。
PLoS One. 2013 Jul 5;8(7):e67647. doi: 10.1371/journal.pone.0067647. Print 2013.
7
The Type VI secretion system - a widespread and versatile cell targeting system.VI 型分泌系统——一种广泛而通用的细胞靶向系统。
Res Microbiol. 2013 Jul-Aug;164(6):640-54. doi: 10.1016/j.resmic.2013.03.017. Epub 2013 Mar 27.
8
Imaging type VI secretion-mediated bacterial killing.成像技术揭示 VI 型分泌系统介导的细菌杀伤机制
Cell Rep. 2013 Jan 31;3(1):36-41. doi: 10.1016/j.celrep.2012.11.027. Epub 2013 Jan 3.
9
ClpV recycles VipA/VipB tubules and prevents non-productive tubule formation to ensure efficient type VI protein secretion.ClpV 回收 VipA/VipB 小管并防止非生产性小管形成,以确保有效的 VI 型蛋白分泌。
Mol Microbiol. 2013 Mar;87(5):1013-28. doi: 10.1111/mmi.12147. Epub 2013 Feb 3.
10
Structure and regulation of the type VI secretion system.VI 型分泌系统的结构与调控。
Annu Rev Microbiol. 2012;66:453-72. doi: 10.1146/annurev-micro-121809-151619. Epub 2012 Jun 28.

VI 型分泌系统和噬菌体尾管共享一个共同的组装途径。

Type VI secretion and bacteriophage tail tubes share a common assembly pathway.

机构信息

Laboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée CNRS - UMR 7255 Aix-Marseille University, Marseille, France.

出版信息

EMBO Rep. 2014 Mar;15(3):315-21. doi: 10.1002/embr.201337936. Epub 2014 Jan 31.

DOI:10.1002/embr.201337936
PMID:24488256
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3989698/
Abstract

The Type VI secretion system (T6SS) is a widespread macromolecular structure that delivers protein effectors to both eukaryotic and prokaryotic recipient cells. The current model describes the T6SS as an inverted phage tail composed of a sheath-like structure wrapped around a tube assembled by stacked Hcp hexamers. Although recent progress has been made to understand T6SS sheath assembly and dynamics, there is no evidence that Hcp forms tubes in vivo. Here we show that Hcp interacts with TssB, a component of the T6SS sheath. Using a cysteine substitution approach, we demonstrate that Hcp hexamers assemble tubes in an ordered manner with a head-to-tail stacking that are used as a scaffold for polymerization of the TssB/C sheath-like structure. Finally, we show that VgrG but not TssB/C controls the proper assembly of the Hcp tubular structure. These results highlight the conservation in the assembly mechanisms between the T6SS and the bacteriophage tail tube/sheath.

摘要

VI 型分泌系统(T6SS)是一种广泛存在的大分子结构,可将蛋白效应器输送到真核和原核受体细胞。目前的模型将 T6SS 描述为一个倒置的噬菌体尾部,由一个鞘状结构包裹在由堆叠的 Hcp 六聚体组装而成的管周围。尽管最近在理解 T6SS 鞘的组装和动力学方面取得了进展,但没有证据表明 Hcp 在体内形成管。在这里,我们表明 Hcp 与 T6SS 鞘的组成部分 TssB 相互作用。通过半胱氨酸取代方法,我们证明 Hcp 六聚体以有序的方式组装成管状结构,头对头堆叠,作为 TssB/C 鞘状结构聚合的支架。最后,我们表明 VgrG 而不是 TssB/C 控制 Hcp 管状结构的正确组装。这些结果强调了 T6SS 和噬菌体尾部管/鞘之间在组装机制上的保守性。