Abstract
In Xenopus oocytes, 5S rRNA is exported out of the nucleus in the context of two ribonucleoprotein complexes (RNPs): complexed with transcription factor IIIA as the 7S RNP or as the 5S RNP with ribosomal protein L5. 5S rRNA-containing RNP export takes place at a slow rate in comparison to that of nuclear export signal-containing proteins and the U1 snRNP. Using oocyte microinjection assays we found that the export of 5S RNPs requires nuclear RanGTP and RanGTP hydrolysis and is leptomycin B-sensitive, indicating the process is mediated by the export receptor CRM1. A novel nuclear export signal motif is characterised in a region of L5 also possessing a nuclear import signal, thus identifying a shuttling domain for this protein. This same motif in L5 is found to be required for interaction with CRM1 in vitro and for export in vivo.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Active Transport, Cell Nucleus / physiology*
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Amino Acid Sequence / genetics
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Animals
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Cell Nucleus / enzymology*
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Eukaryotic Cells / enzymology*
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Exportin 1 Protein
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Female
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Guanosine Diphosphate / genetics
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Guanosine Diphosphate / metabolism
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Guanosine Triphosphate / genetics
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Guanosine Triphosphate / metabolism
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Karyopherins / genetics
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Karyopherins / metabolism*
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Oocytes
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Protein Structure, Tertiary / genetics
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RNA, Ribosomal, 5S / genetics
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RNA, Ribosomal, 5S / metabolism*
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RNA, Small Cytoplasmic / genetics
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RNA, Small Cytoplasmic / metabolism
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Receptors, Cytoplasmic and Nuclear*
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Ribonucleoproteins / genetics
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Ribonucleoproteins / metabolism*
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Signal Recognition Particle / genetics
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Signal Recognition Particle / metabolism
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Time Factors
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Xenopus laevis
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ran GTP-Binding Protein / genetics
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ran GTP-Binding Protein / metabolism*
Substances
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7SL RNA
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Karyopherins
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RNA, Ribosomal, 5S
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RNA, Small Cytoplasmic
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Receptors, Cytoplasmic and Nuclear
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Ribonucleoproteins
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Signal Recognition Particle
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Guanosine Diphosphate
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Guanosine Triphosphate
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ran GTP-Binding Protein