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Fig. 2. Functional domains in ARSs and ARS-related factors. The domains homologous to glutathione S-transferase (GST; red boxes) are shown in the N-terminal regions of MRS, EPRS and VRS, as well as in the C-terminal regions of p18 and p38. p38 also contains a leucine zipper motif (violet box) and is involved in macromolecular assembly of ARSs (Quevillon et al., 1999; Ahn et al., 2003). The sequence similarity between the helical tRNA-binding domain (green boxes) of MRS, GRS, HRS, WRS and the three repeated domains of EPRS was revealed by sequence alignment (Kaminska et al., 2001). Interestingly, these motifs are also involved in protein-protein interactions (Rho et al., 1996; Rho et al., 1998). DRS and KRS also contain helical tRNA-binding domains (TRBD; blue boxes), although they are not related to the motif mentioned above (Frugier et al., 2000; Francin et al., 2002). By contrast, the oligonucleotide-binding (OB) fold domains (blue boxes) in p43 and YRS are related (Renault et al., 2001). The similar RNA-binding OB folds can also be detected in some ARSs (human DRS, KRS and NRS; Escherichia coli MRS and FRS ß-subunit) and other proteins (Arc1p, Trbp111, EF-1ß and EF-1).

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