| 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 | | |
