Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2048481 | FEBS Letters | 2012 | 5 Pages |
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.