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

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...

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Bibliographic Details
Published in:Biochemical journal 2000-02, Vol.346 Pt 1 (1), p.107-115
Main Authors: Kruse, C, Willkomm, D K, Grünweller, A, Vollbrandt, T, Sommer, S, Busch, S, Pfeiffer, T, Brinkmann, J, Hartmann, R K, Müller, P K
Format: Article
Language:English
Subjects:
Animals
Biological Transport
Blotting, Western
Carrier Proteins - chemistry
Carrier Proteins - metabolism
Cell Nucleus - chemistry
Cell Nucleus - metabolism
Cells, Cultured
Cytoplasm - chemistry
Cytoplasm - metabolism
Elongation factor EF-1a
exportin-t
Fibroblasts
hnRNA
Humans
Kinetics
Microscopy, Fluorescence
Models, Biological
Molecular Weight
Nucleocytoplasmic Transport Proteins
Peptide Elongation Factor 1 - chemistry
Peptide Elongation Factor 1 - metabolism
Protein Binding
Recombinant Proteins - administration & dosage
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
RNA, Transfer - administration & dosage
RNA, Transfer - genetics
RNA, Transfer - metabolism
RNA-Binding Proteins - administration & dosage
RNA-Binding Proteins - genetics
RNA-Binding Proteins - metabolism
Substrate Specificity
Thermodynamics
tRNA
Tumor Cells, Cultured
Vigilin
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Description
Summary: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)-1alpha is enriched in VCC(N) and its cytoplasmic counterpart VCC(C), whereas EF-1beta, EF-1gamma and EF-1delta 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 multi-protein complexes containing tRNA.
ISSN:0264-6021
1470-8728
DOI:10.1042/0264-6021:3460107