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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Conjugative coupling proteins interact with cognate and heterologous VirB10-like proteins while exhibiting specificity for cognate relaxosomes.
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Conjugative coupling proteins interact with cognate and heterologous VirB10-like proteins while exhibiting specificity for cognate relaxosomes.

机译：共轭偶联蛋白与同源和异源VirB10样蛋白相互作用，同时表现出对同源弛豫小体的特异性。

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摘要

Conjugative coupling proteins (CPs) are proposed to play a role in connecting the relaxosome to a type IV secretion system (T4SS) during bacterial conjugation. Here we present biochemical and genetic evidence indicating that the prototype CP, TrwB, interacts with both relaxosome and type IV secretion components of plasmid R388. The cytoplasmic domain of TrwB immobilized in an affinity resin retained TrwC and TrwA proteins, the components of R388 relaxosome. By using the bacterial two-hybrid system, a strong interaction was detected between TrwB and TrwE, a core component of the conjugative T4SS. This interaction was lost when the transmembrane domains of either TrwB or TrwE were deleted, thus suggesting that it takes place within the membrane or periplasmic portions of both proteins. We have also analyzed the interactions with components of the related IncN plasmid pKM101. Its CP, TraJ, did not interact with TrwA, suggesting a highly specific interaction with the relaxosome. On the other side, CPs fromthree different conjugation systems were shown to interact with both their cognate TrwE-like component and the heterologous ones, suggesting that this interaction is less specific. Mating experiments among the three systems confirmed that relaxosome components need their cognate CP for transfer, whereas T4SSs are interchangeable. As a general rule, there is a correlation between the strength of the interaction seen by two-hybrid analysis and the efficiency of transfer.
机译：提出了偶联偶联蛋白（CPs）在细菌偶联过程中在将弛豫体与IV型分泌系统（T4SS）连接中发挥作用。在这里，我们提供了生化和遗传证据，表明原型CP，TrwB与质粒R388的弛豫体和IV型分泌成分相互作用。固定在亲和树脂中的TrwB的胞质结构域保留了TrwC和TrwA蛋白（R388弛豫体的成分）。通过使用细菌双杂交系统，在TrwB和TrwE（共轭T4SS的核心组成部分）之间检测到强相互作用。当删除TrwB或TrwE的跨膜结构域时，这种相互作用就会消失，因此表明它发生在两种蛋白质的膜或周质部分内。我们还分析了与相关IncN质粒pKM101的成分之间的相互作用。它的CP，TraJ，与TrwA不相互作用，表明与松弛体具有高度特异性的相互作用。另一方面，显示来自三个不同共轭系统的CP与它们的同类TrwE样成分和异源成分都相互作用，这表明这种相互作用的特异性较低。这三个系统之间的交配实验证实，松弛体组分需要其同源CP才能转移，而T4SS是可互换的。通常，通过双杂交分析看到的相互作用强度与转移效率之间存在相关性。

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