ePrints

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

Lookup NU author(s): Dr Heather Lamb, Professor Alastair Hawkins

Downloads

Full text for this publication is not currently held within this repository. Alternative links are provided below where available.

Abstract

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: mbeA and mbeC physically interact by two hybrid (View interaction) mbeA and mbeC bind by isothermal titration calorimetry (View interaction) (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Publication metadata

Author(s): Varsaki A, Lamb HK, Eleftheriadou O, Vandera E, Thompson P, Moncalian G, de la Cruz F, Hawkins AR, Drainas C

Publication type: Article

Publication status: Published

Journal: FEBS Letters

Year: 2012

Volume: 586

Issue: 6

Pages: 675-679

Print publication date: 01/03/2012

ISSN (print): 0014-5793

ISSN (electronic): 1873-3468

Publisher: Elsevier BV

URL: http://dx.doi.org/10.1016/j.febslet.2012.01.060

DOI: 10.1016/j.febslet.2012.01.060

Altmetrics

Share