Figure 5. Sub2-activated conformation at the proximal side of the THO homodimer.

(A) Sub2-Tho2 interaction at the proximal side. The zoom views show a subset of conserved interacting residues. See also Figure 3—figure supplements 2 and 5. (B) Structure of DDX6-CNOT1-4ET (Ozgur et al., 2015a) shown in the same orientation as Sub2-Tho2 in panel A after superposition of their RecA2 domains. Note that the Tho2 ‘handle’ binds RecA2 at the equivalent position as protein 4E-T.

Figure 5—figure supplement 1. Conformational states of Sub2.

Comparison of the activated semi-closed Sub2 structure as found at the proximal side of the THO homodimer cryo-electron microscopy structure with the conformation of active Sub2, bound to RNA, nucleotide, and the C-terminal motif of Yra1 (C-box) (Ren et al., 2017). All structures are aligned on the N-terminal RecA1 domain. The RecA1 domain is colored in light-pink, the RecA2 in purple, and Yra1 in gray. RNA is shown in black and nucleotide in yellow.