1r1b

Publication Abstract from PubMed

Aminoacyl-tRNA synthetases of higher eukaryotes possess polypeptide extensions in contrast to their prokaryotic counterparts. These extra domains of poorly understood function are believed to be involved in protein-protein or protein-RNA interactions. Here we showed by gel retardation and filter binding experiments that the repeated units that build the linker region of the bifunctional glutamyl-prolyl-tRNA synthetase had a general RNA-binding capacity. The solution structure of one of these repeated motifs was also solved by NMR spectroscopy. One repeat is built around an antiparallel coiled-coil. Strikingly, the conserved lysine and arginine residues form a basic patch on one side of the structure, presenting a suitable docking surface for nucleic acids. Therefore, this repeated motif may represent a novel type of general RNA-binding domain appended to eukaryotic aminoacyl-tRNA synthetases to serve as a cis-acting tRNA-binding cofactor.

A recurrent RNA-binding domain is appended to eukaryotic aminoacyl-tRNA synthetases.,Cahuzac B, Berthonneau E, Birlirakis N, Guittet E, Mirande M EMBO J. 2000 Feb 1;19(3):445-52. PMID:10654942^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.