Expert and transport of tRNA are coupled to a multi-protein complex

Charli Kruse*, Dagmar K. Willkomm, Arnold Grünweller, Tillmann Vollbrandt, Stefanie Sommer, Silke Busch, Thomas Pfeiffer, Jürgen Brinkmann, Roland K. Hartmann, Peter K. Müller

*Corresponding author for this work
39 Citations (Scopus)


Vigilin is a ubiquitous multi heterogeneous nuclear ribonucleoprotein (hnRNP) K homologous (KH)-domain protein. Here we demonstrate that purified recombinant human vigilin binds tRNA molecules with high affinity, although with limited specificity. Nuclear microinjection experiments revealed for the first time that the immuno-affinity-purified nuclear vigilin core complex (VCC(N)) as well as recombinant vigilin accelerate tRNA export from the nucleus in human cells. The nuclear tRNA receptor exportin-t is part of the VCC(N). Elongation factor (EF)-1α is enriched in VCC(N) and its cytoplasmic counterpart VCC(C), whereas EF-1β, EF-1γ and EF-1δ are basically confined to the VCC(C). Our results suggest further that vigilin and exportin-t might interact during tRNA export, provide evidence that the channeled tRNA cycle is already initiated in the nucleus, and illustrate that intracellular tRNA trafficking is associated with discrete changes in the composition of cellular cytoplasmic multiprotein complexes containing tRNA.

Original languageEnglish
JournalBiochemical Journal
Issue number1
Pages (from-to)107-115
Number of pages9
Publication statusPublished - 15.02.2000

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)


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