Fig. 3.

Vms1p is structurally homologous to tRNA hydrolases. a Domain structure of Vms1p. LRS leucine-rich sequence, ZnF zinc finger, MTD/eRFL mitochondrial targeting domain/eRF1-like, AnkR ankryin repeat, CC coil–coil, VIM VCP-interacting motif. Residues 188–417 represent the MTD/eRFL boundaries. b Structural alignment of Vms1p (left, 5WHG³¹) and eRF1p (middle, 3JAHii³⁵, residues 144–280). Dashed lines indicate connections made by residues that are not resolved in the Vms1p crystal structure. The GGQ (red) loop of eRF1p is ordered in the ribosome-bound structure shown here. c Sequence alignment of Vms1p and eRF1p. White letters with gray, black, or red background indicates similarity, identity, or GxxQ residues, respectively. d Sequence alignment of Vms1p orthologs across the GxxQ region. Coloring as in c. e, f Serial dilutions of indicated strains were spotted on media containing glucose or glucose supplemented with cycloheximide (CHX). EV empty vector