Abstract
The binding of tRNA species from calf liver to immobilized exportin-t in the presence of ran•GppNHp was examined by affinity chromatography. We observed different eluting behaviors of individual tRNAs. After separating tRNAs on a two-dimensional polyacrylamide gel, the positions of 7 selected tRNAs were identified by Northern hybridization and their relative affinities to immobilized exportin-t•ran•GppNHp complex were estimated in the order of tRNALeuCAG > tRNASerGCU, tRNALeuCAA, tRNASerUGA > tRNASerAGA, tRNALeuAAG > tRNAArgACG. We propose that exportin-t preferentially binds and exports those tRNAs that are rapidly consumed by the protein synthesis machinery.
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