Interaction between relaxase MbeA and accessory protein MbeC of the conjugally mobilizable plasmid ColE1

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• 作者：Athanasia Varsaki^a ; ¹ ; ^{avarsaki@gmail.com} ; Heather K. Lamb^b ; ¹ ; Olga Eleftheriadou^a ; Elpiniki Vandera^a ; Paul Thompson^b ; Gabriel Moncaliá ; n^c ; Fernando de la Cruz^c ; Alastair R. Hawkins^b ; ^{a.r.hawkins@ncl.ac.uk} ; Constantin Drainas^a
• 关键词：Bacterial conjugation ; Plasmid mobilization ; Protein interaction ; Relaxase ; Accessory protein ; ColE1 plasmid
• 刊名：FEBS Letters
• 出版年：2012
• 期刊代码：70_00145793
• 类别：bio
• 出版时间：23 March, 2012
• 卷：586
• 期：6
• 页码：675-679
• 文件大小：575 K

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

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