Drawing on disorder: How viruses use histone mimicry to their advantage

Tarakhovsky, Alexander; Prinjha, Rab K.

In the H3N2 strain, the presence of the histone mimic may contribute to the unique ability of the virus to compete with the cognate histone sequences for their common binding partners, including those that drive antiviral gene expression. In support of this model, we found that both the histone H3 tail and the H3N2 NS1 tail bind in a sequence-dependent fashion to the polymerase-associated factor 1 (Paf1) component of the Paf1 complex that contributes to RNA elongation as well as other cotranscriptional processes (Marazzi et al., 2012) . As expected, the NS1 tails from influenza H5N1 (Marazzi et al., 2012) and H1N1 (Schaefer et al., 2013) that lack the histone mimic did not bind to Paf1.