Rpn11p is recruited to the tombusvirus replicase in yeast.

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Rpn11p is recruited to the tombusvirus replicase in yeast. Rpn11p is recruited to the tombusvirus replicase in yeast. (A and B) Interaction between Rpn11p and the TBSV p92 replication protein. A split-ubiquitin assay was used to test binding between either p33 (A) or p92 (B) and the shown full-length yeast proteins. The bait p33 or p92 was coexpressed with the prey proteins in yeast. Ssa1p (HSP70 chaperone) and the empty prey vector (NubG, shown by a dash) were used as positive and negative controls, respectively. The image shows results for 10-fold serial dilutions of yeast cultures. (C) Copurification of Rpn11p with the p33 and p92 replication proteins from yeast. The FLAG-tagged p33 or FLAG-p92 was purified from a solubilized membranous fraction of yeast extracts using a FLAG affinity column (lanes 2 to 4 and 6 to 8). The 6×His-tagged p33 purified using a FLAG affinity column (lanes 1 and 5) was used as a negative control. (Top) Western blot analysis of 6×His-tagged Rpn11p with anti-His antibody in the affinity-purified preparations. (Middle) Western blot analysis of the same samples as in the top portion but using anti-FLAG antibody. (Bottom) Western blot analysis of 6×His-tagged p33 and 6×His-Rpn11 with anti-His antibody in the total protein extract from yeast expressing the shown proteins. Each experiment was repeated three times. K. Reddisiva Prasanth et al. J. Virol. 2015;89:2750-2763