Scientific article
Open access

Identification of a tRNA-specific nuclear export receptor

Published inMolecular cell, vol. 1, no. 3, p. 359-369
Publication date1998-02

In eukaryotes, tRNAs are synthesized in the nucleus and after several maturation steps exported to the cytoplasm. Here, we identify exportin-t as a specific mediator of tRNA export. It is a RanGTP-binding, importin beta-related factor with predominantly nuclear localization. It shuttles rapidly between nucleus and cytoplasm and interacts with nuclear pore complexes. Exportin-t binds tRNA directly and with high affinity. Its cellular concentration in Xenopus oocytes was found to be rate-limiting for export of all tRNAs tested, as judged by microinjection experiments. RanGTP regulates the substrate-exportin-t interaction such that tRNA can be preferentially bound in the nucleus and released in the cytoplasm.

  • Amino Acid Sequence
  • Animals
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism
  • Cell Nucleus / chemistry
  • Cell Nucleus / metabolism
  • Cloning, Molecular
  • Cytoplasm / metabolism
  • GTP-Binding Proteins / metabolism
  • GTPase-Activating Proteins
  • HeLa Cells
  • Humans
  • Molecular Sequence Data
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism
  • Nucleocytoplasmic Transport Proteins
  • Oocytes / physiology
  • Protein Binding / physiology
  • RNA, Messenger / analysis
  • RNA, Transfer / metabolism
  • RNA, Transfer, Amino Acid-Specific / metabolism
  • RNA, Transfer, Leu / metabolism
  • RNA, Transfer, Ser / metabolism
  • Xenopus
  • Xenopus Proteins
  • Beta Karyopherins
  • Ran GTP-Binding Protein
Citation (ISO format)
KUTAY, Ulrike et al. Identification of a tRNA-specific nuclear export receptor. In: Molecular cell, 1998, vol. 1, n° 3, p. 359–369. doi: 10.1016/s1097-2765(00)80036-2
Main files (1)
Article (Published version)
ISSN of the journal1097-2765

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