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首页> 外文期刊>FEBS letters. >Interaction between relaxase MbeA and accessory protein MbeC of the conjugally mobilizable plasmid ColE1
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Interaction between relaxase MbeA and accessory protein MbeC of the conjugally mobilizable plasmid ColE1

机译:接合酶可动员质粒ColE1的松弛酶MbeA与辅助蛋白MbeC之间的相互作用

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摘要

MbeA and MbeC are two key proteins in plasmid ColE1 conjugal mobilization. Isothermal titration calorimetry was used to detect and quantify an interaction between MbeA and MbeC. As a result of this interaction, the affinity of MbeA for single stranded DNA increased. The interaction was confirmed in vivo using a bacterial two-hybrid system, which revealed that MbeA-MbeC complexes are formed through the amino-terminal region of MbeA and the carboxy-terminal region of MbeC. To the best of our knowledge, this is the first report of direct interactions between conjugative proteins encoded by a mobilizable plasmid. Structured summary of protein interactions: mbeA and mbeC physically interact by two hybrid (View interaction) mbeA and mbeC bind by isothermal titration calorimetry (View interaction).
机译:MbeA和MbeC是质粒ColE1结合动员中的两个关键蛋白。等温滴定热法用于检测和定量MbeA和MbeC之间的相互作用。这种相互作用的结果是,MbeA对单链DNA的亲和力增加。使用细菌双杂交系统在体内证实了相互作用,这揭示了MbeA-MbeC复合物是通过MbeA的氨基末端区域和MbeC的羧基末端区域形成的。据我们所知,这是关于由可动员质粒编码的结合蛋白之间直接相互作用的首次报道。蛋白质相互作用的结构总结:mbeA和mbeC通过两个杂合体(视图相互作用)进行物理相互作用(通过等温滴定量热法(视图相互作用)进行结合)。

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