Structures of the tRNA export factor in the nuclear and cytosolic states

Atlanta G. Cook, Noemi Fukuhara, Martin Jinek and Elena Conti ()
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Atlanta G. Cook: Structural Cell Biology, MPI for Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
Noemi Fukuhara: EMBL, Meyerhofstrasse 1, Heidelberg D69117, Germany
Martin Jinek: EMBL, Meyerhofstrasse 1, Heidelberg D69117, Germany
Elena Conti: Structural Cell Biology, MPI for Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany

Nature, 2009, vol. 461, issue 7260, 60-65

Abstract: Abstract Transfer RNAs are among the most ubiquitous molecules in cells, central to decoding information from messenger RNAs on translating ribosomes. In eukaryotic cells, tRNAs are actively transported from their site of synthesis in the nucleus to their site of function in the cytosol. This is mediated by a dedicated nucleo-cytoplasmic transport factor of the karyopherin-β family (Xpot, also known as Los1 in Saccharomyces cerevisiae). Here we report the 3.2 Å resolution structure of Schizosaccharomyces pombe Xpot in complex with tRNA and RanGTP, and the 3.1 Å structure of unbound Xpot, revealing both nuclear and cytosolic snapshots of this transport factor. Xpot undergoes a large conformational change on binding cargo, wrapping around the tRNA and, in particular, binding to the tRNA 5′ and 3′ ends. The binding mode explains how Xpot can recognize all mature tRNAs in the cell and yet distinguish them from those that have not been properly processed, thus coupling tRNA export to quality control.

Date: 2009
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DOI: 10.1038/nature08394

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