Figure 8.

Features of (A) minimal and (B) optimal RNA substrates for Ebola VP30. (C) Sketch of the proposed RNA binding interface. VP30 is shown as a trimer of dimers, taking into account that the protein's capability to form hexamers is essential for gel-resolvable RNA binding.³³ As a consequence, the RNA binding path is tentatively indicated at the interface between dimers. While short ssRNAs (∼14 nt) rapidly dissociate from VP30, as inferred from the absence of gel-resolvable complexes in the case of a ssRNA 14-mer (Fig. 7), longer RNAs bind more stably, further supported by a stem-loop structure particularly at the 3′-end.