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

Atlanta G Cook, Noemi Fukuhara, Martin Jinek, Elena Conti

Research output: Contribution to journalArticlepeer-review


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-beta family (Xpot, also known as Los1 in Saccharomyces cerevisiae). Here we report the 3.2 A resolution structure of Schizosaccharomyces pombe Xpot in complex with tRNA and RanGTP, and the 3.1 A 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.
Original languageEnglish
Pages (from-to)60-65
Number of pages6
Issue number7260
Publication statusPublished - 3 Sep 2009


  • Binding Sites
  • Cell Nucleus
  • Crystallography, X-Ray
  • Cytosol
  • GTPase-Activating Proteins
  • Models, Molecular
  • Nuclear Pore Complex Proteins
  • Protein Binding
  • Protein Conformation
  • RNA Transport
  • RNA, Fungal
  • RNA, Transfer
  • RNA, Transfer, Phe
  • Saccharomyces cerevisiae Proteins
  • Schizosaccharomyces pombe Proteins
  • Substrate Specificity
  • ran GTP-Binding Protein


Dive into the research topics of 'Structures of the tRNA export factor in the nuclear and cytosolic states'. Together they form a unique fingerprint.

Cite this