Models showing the proposed function of subverted cellular Rpn11p metalloprotease in TBSV replication and viral RNA recombination. Models showing the proposed.

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Models showing the proposed function of subverted cellular Rpn11p metalloprotease in TBSV replication and viral RNA recombination. Models showing the proposed function of subverted cellular Rpn11p metalloprotease in TBSV replication and viral RNA recombination. (Left) Rpn11p is proposed to facilitate the efficient recruitment of the cellular DDX3-like Ded1/AtRH20 helicases together with the viral p92pol replication protein into the VRCs. This activity of Rpn11p makes the properly assembled VRCs efficient in viral RNA replication and also results in suppression of RNA recombination. Note that AtRH20 is a functional ortholog of the yeast Ded1 in TBSV replication. (Right) When Rpn11p is depleted or mutated, then recruitment of Ded1/AtRH20 helicases into the VRCs is inefficient. This alters the VRC components, leading to low replication but highly efficient template-switching-type viral RNA recombination. Together, these models propose key recruitment and VRC assembly functions for the co-opted Rpn11p during TBSV replication and recombination. K. Reddisiva Prasanth et al. J. Virol. 2015;89:2750-2763