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

Author

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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
    Present addresses: Division of Cell and Molecular Biology, Biophysics section, Blackett Laboratory, Imperial College London, London SW7 2AZ, UK (N.F.); Department of Molecular Cell Biology, University of California at Berkeley, 731 Stanley Hall, Berkeley, California 94720, USA (M.J.).)

  • Martin Jinek

    (EMBL, Meyerhofstrasse 1, Heidelberg D69117, Germany
    Present addresses: Division of Cell and Molecular Biology, Biophysics section, Blackett Laboratory, Imperial College London, London SW7 2AZ, UK (N.F.); Department of Molecular Cell Biology, University of California at Berkeley, 731 Stanley Hall, Berkeley, California 94720, USA (M.J.).)

  • Elena Conti

    (Structural Cell Biology, MPI for Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    EMBL, Meyerhofstrasse 1, Heidelberg D69117, Germany)

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.

Suggested Citation

  • Atlanta G. Cook & Noemi Fukuhara & Martin Jinek & Elena Conti, 2009. "Structures of the tRNA export factor in the nuclear and cytosolic states," Nature, Nature, vol. 461(7260), pages 60-65, September.
    • Handle: RePEc:nat:nature:v:461:y:2009:i:7260:d:10.1038_nature08394
    DOI: 10.1038/nature08394
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    Cited by:

    1. Aline Umuhire Juru & Rodolfo Ghirlando & Jinwei Zhang, 2024. "Structural basis of tRNA recognition by the widespread OB fold," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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