Immunoblotting (IB) analysis of the protein complex with anti-MurG, anti-MreB and anti-β-lactamase under non-reducing conditions

<p><b>Copyright information:</b></p><p>Taken from "The essential peptidoglycan glycosyltransferase MurG forms a complex with proteins involved in lateral envelope growth as well as with proteins involved in cell division in "</p><p></p><p>Molecular Microbiology 2007;65(4):1106-1121.</p><p>Published online Jan 2007</p><p>PMCID:PMC2170320.</p><p>© 2007 The Authors; Journal compilation © 2007 Blackwell Publishing Ltd</p> The membranes extracted from BW25113Δ/pMAKec strain (MraY–β-lactamase–His expressing strain) were used for the IP (with cross-linking) with anti-MurG. The blot was then probed with anti-MurG (lanes 1 and 2), anti-MreB (lanes 3 and 4) or anti β-lactamase (lanes 5 and 6). In parallel the same IP was performed without the membrane fraction (lanes 1, 3 and 5). A cross-linked product with a molecular weight of about 120 kDa is visible in all samples except in control samples (lanes 1, 3 and 5). The faint band in lane 2 is MurG, which is not completely cross-linked in the protein complex. The band in lane 6 with the molecular weight of approximately 70 kDa corresponds to the MraY–β-lactamase–His protein that is not completely cross-linked in the protein complex