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. 2017 Oct 23;13(10):e1006689. doi: 10.1371/journal.ppat.1006689

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© 2017 Prasanth 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 credited.

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Fig 1 — (A) Co-purification of Pgk1 with the viral replicase. Top panel: Western blot analysis of co-purified His₆-tagged Pgk1 with FLAG-affinity purified FLAG-p33 and FLAG-p92^pol from membrane fraction of yeast. Pgk1 was detected with anti-His antibody. The negative control was His₆-tagged p33 and His₆-p92 purified from yeast extracts using a FLAG-affinity column. Middle panel: Western blot of purified FLAG-p33 and FLAG-p92^pol detected with anti-FLAG antibody. Asterisk marks the SDS-resistant p33 homodimer. Bottom panel: Western blot of His₆-tagged Pgk1 and His₆-p33 (lane 1) proteins in the total yeast extracts using anti-His antibody. (B) Testing the presence of Pgk1 in the membrane-bound viral replicase after blocking cellular translation by cycloheximide. Top panel: Western blot analysis shows the co-purified His₆-tagged Pgk1 with the viral replicase isolated from membrane fraction at the shown time points. See further details in panel A. Middle panel: Western blot analysis of the purified FLAG-p33 with anti-FLAG antibody. Bottom panel: Western blot analysis of His₆-Pgk1 in the total yeast lysates with anti-His antibody. Each experiment was repeated three times.