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Interaction between relaxase MbeA and accessory protein MbeC of the conjugally mobilizable plasmid ColE1. Interaction between relaxase MbeA and accessory protein MbeC of the conjugally mobilizable plasmid ColE1. Varsaki A, Lamb HK, Eleftheriadou O, Vandera E, Thompson P, Moncalián G, de la Cruz F, Hawkins AR, Drainas C. FEBS Lett. 2012 Mar 23;586(6):675-9.2012-03-14T23:00:00Z<p><span class="ms-rteThemeFontFace-1 ms-rteFontSize-2"><span class="ms-rteThemeForeColor-2-5 ms-rteThemeFontFace-1 ms-rteFontSize-2" style="font-weight:bold;">Abstract</span><br></span></p><div style="color:#000000;font-family:arial, helvetica, clean, sans-serif;"><p style="margin-bottom:0.5em;font-size:1.04em;"><span class="ms-rteThemeFontFace-1 ms-rteFontSize-2">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.</span><br></p></div><p>​<span style="color:#474f51;font-family:"yanone kaffeesatz";font-size:18px;background-color:#ffffff;">[</span><a href="http://www.ncbi.nlm.nih.gov/pubmed/22449962" style="color:#ed391b;margin:0px;padding:0px;border:0px;font-stretch:inherit;font-size:18px;line-height:inherit;font-family:"yanone kaffeesatz";vertical-align:baseline;background-color:#ffffff;">pubmed</a><span style="color:#474f51;font-family:"yanone kaffeesatz";font-size:18px;background-color:#ffffff;">]</span><br></p>95

 
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