G. Simos et al., THE YEAST PROTEIN ARC1P BINDS TO TRANSFER-RNA AND FUNCTIONS AS A COFACTOR FOR THE METHIONYL-TRANSFER-RNA AND GLUTAMYL-TRANSFER-RNA SYNTHETASES, EMBO journal, 15(19), 1996, pp. 5437-5448
Arc1p was found in a screen for components that interact genetically w
ith Los1p, a nuclear pore-associated yeast protein involved in tRNA bi
ogenesis. Arc1p is associated with two proteins which were identified
as methionyl-tRNA and glutamyl-tRNA synthetase (MetRS and GluRS) by a
new mass spectrometry method, ARC1 gene disruption leads to slow growt
h and reduced MetRS activity, and synthetically lethal arc1(-) mutants
are complemented by the genes for MetRS and GluRS, Recombinant Arc1p
binds in vitro to purified monomeric yeast MetRS, but not to an N-term
inal truncated form, and strongly increases its apparent affinity for
tRNA(Met), Furthermore, Arclp, which is allelic to the quadruplex nucl
eic acid binding protein G4p1, exhibits specific binding to tRNA as de
termined by gel retardation and UV-cross-linking, Arclp is, therefore,
a yeast protein with dual specificity: it associates with tRNA and am
inoacyl-tRNA synthetases, This functional interaction may be required
for efficient aminoacylation in vivo.