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

Tarakhovsky, Alexander; Prinjha, Rab K.

Intrinsically disordered proteins (IDPs) in virushost interactions It appears that viruses are well equipped to implement a multitarget strategy toward interference with multiple cell functions. At the foundation of this viral feature is the abundance of potentially polyreactive IDPs or intrinsically disordered regions (IDRs) in the viral proteome (Dunker et al., 2000 (Dunker et al., , 2001 Tompa, 2002; Uversky, 2002; Ward et al., 2004; Uversky and Dunker, 2010) . IDPs/IDRs, which are also common in the mammalian proteome, are characterized by high proportions of charged and hydrophilic amino acids combined with a low abundance of bulky hydrophobic amino acids. The IDP are unable to fold spontaneously into stable three-dimensional globular structures and (Dyson and Wright, 2005) . This feature allows IDPs to form dynamically heterogeneous complexes with multiple binding partners (Ferreon et al., 2009; Ishiyama et al., 2010) . The dynamic nature of most IDPs also allows for increased availability of binding sites, with binding diversity greatly augmented by the propensity of IDPs to be posttranslationally modified (Gibson, 2009 ). These features contribute to the governing role of IDPs in signaling networks Dyson and Wright, 2005; Ishiyama et al., 2010) . IDRs participate in the assembly of numerous signaling complexes through reversible protein-protein interactions that promote formation of either fully reversible cellular assemblies or stable amyloid scaffolds (Li et al., 2012) .