کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2048481 | 1074082 | 2012 | 5 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: 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](/preview/png/2048481.png)
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 interactionsmbeA and mbeCphysically interact by two hybrid (View interaction)mbeA and mbeCbind by isothermal titration calorimetry (View interaction)
► ITC was used to detect and quantify interaction between MbeA_ColE1 and MbeC_ColE1.
► The MbeA–MbeC interaction increases the affinity of MbeA for ssDNA.
► The interaction was confirmed in vivo using a 2HB system.
► The complexes are formed through the MbeA N-terminal and the MbeC C-terminal region.
► This is the first report of direct protein-interactions from a mobilizable plasmid.
Journal: FEBS Letters - Volume 586, Issue 6, 23 March 2012, Pages 675–679