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Fig. 3. A schematic hypothetical model for the organization of mammalian, yeast and archea tRNA synthetase complexes. (A) The two-dimensional arrangement of the components in the mammalian multi-ARS synthetase complex. p38 is a scaffold protein for the assembly of the components. Some of the interactions, which have been determined by two-hybrid analyses (Rho et al., 1996; Quevillon et al., 1999) and crosslinking methods (Norcum and Warrington, 1998), are shown as arrows in this diagram. Owing to the limits of two-dimensional display, some interactions are not shown. (B) The yeast ARS complex consisting of two ARSs (MRS and ERS) and Arc1p, the yeast homolog of mammalian p43. Both ARSs interact directly with the N-terminal domain of Arc1p through their N-terminal appended domains (Galani et al., 2001). (C) The putative metabolic protein Mj1338 copurified with PRS from Methanococcus jannaschii interacts with KRSs from human and Methanobacterium thermoautotropicum in pull-down assays. Its interaction with DRS was also confirmed through identification of aminoacylation activity in a DEAE fraction obtained from total cell lysate of M. jannaschii (Lipman et al., 2000; Lipman et al., 2003). Although some components in these complexes have the potential for homodimerization, for simplicity this is not shown. The spatial arrangements and sizes of the components do not necessarily reflect their relative positions in the complexes.
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