Identification of a nuclear export receptor for tRNA

Abstract

Background: Transport of macromolecules between the nucleus and cytoplasm of eukaryotic cells is mediated by nuclear import and export receptors. The receptors identified to date are members of a family of Ran GTPase-binding proteins whose founding member is importin-beta. Interaction between these receptors and their cargo is regulated by the GTP-bound form of Ran. Export complexes form and import complexes disassemble on binding of RanGTP to the receptor. Yeast Los 1 p is a member of the importin-beta family with a poorly defined role in tRNA production.

Results: A human member of the importin-beta family that is distantly related to Los 1 p (21% identity) has been characterized. The protein shuttled between the nucleus and cytoplasm and interacts with tRNA in a RanGTP-dependent manner. Injection of the protein into the nuclei of Xenopus oocytes resulted in a specific stimulation of the export of tRNA from the nucleus and in relief of the competitive inhibition of tRNA export caused by the introduction of saturating amounts of nuclear tRNA.

Conclusions: The human protein has the functional properties expected of a transport receptor that mediates export of tRNA from the nucleus. We therefore name the protein Exportin(tRNA).