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Journal of Cell Science, Vol 112, Issue 14 2369-2380, Copyright © 1999 by Company of Biologists
JOURNAL ARTICLES |
O Rosorius, B Reichart, F Kratzer, P Heger, MC Dabauvalle and J Hauber
Institute for Clinical and Molecular Virology, University Erlangen-Nurnberg, Schlossgarten 4, D-91054 Erlangen, Germany.
Eukaryotic initiation factor 5A (eIF-5A) is the only cellular protein known to contain the unusual amino acid hypusine. The exact in vivo function of eIF-5A, however, is to date unknown. The finding that eIF-5A is an essential cofactor of the human immunodeficiency virus type 1 (HIV-1) Rev RNA transport factor suggested that eIF-5A is part of a specific nuclear export pathway. In this study we used indirect immunofluorescence and immunogold electron microscopy to demonstrate that eIF-5A accumulates at nuclear pore-associated intranuclear filaments in mammalian cells and Xenopus oocytes. We are able to show that eIF-5A interacts with the general nuclear export receptor, CRM1. Furthermore, microinjection studies in somatic cells revealed that eIF-5A is transported from the nucleus to the cytoplasm, and that this nuclear export is blocked by leptomycin B. Our data demonstrate that eIF-5A is a nucleocytoplasmic shuttle protein.
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