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A recurrent RNA-binding domain is appended to eukaryotic aminoacyl-tRNA synthetases.

ABSTRACT: 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.

SUBMITTER: Cahuzac B

PROVIDER: S-EPMC305581 | biostudies-literature | 2000 Feb

REPOSITORIES: biostudies-literature

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A recurrent RNA-binding domain is appended to eukaryotic aminoacyl-tRNA synthetases.

Cahuzac B B Berthonneau E E Birlirakis N N Guittet E E Mirande M M

The EMBO journal 20000201 3

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 rep ...[more]

PMID: 10654942

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