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. 2014 Aug 28;10(8):e1004552. doi: 10.1371/journal.pgen.1004552

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© 2014 Marmignon et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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(A) Co-precipitation of HA-Ku80c and Ku70a-HA with MBP-Pgm from insect cell extracts (top panel), revealed on western blots using an anti-HA antibody. (B) Co-immunoprecipitation of Pgm with HA-Ku80c and/or Ku70a-HA from insect cell extracts, revealed on western blots using an anti-Pgm antibody. In A and B, the input proteins from each extract are displayed in the bottom panel. (C) The interaction between HA-Ku80c and Pgm is resistant to DNaseI treatment. The co-precipitation experiment was performed as described in A, using MBP-Pgm, HA-Ku80c and 6His-Ku70a recombinant proteins produced from baculovirus vectors. EDTA was removed from the lysis buffer and replaced by 10 mM MgCl₂. Half of the sample was treated with 40 µg/mL of Dnase I during the 2-hr incubation with amylose-coupled magnetic beads. The presence of HA-Ku80c in the purified complexes was revealed on western blots using an anti-HA antibody.