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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1998-7-24
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleocytoplasmic Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RANGAP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Amino Acid-Specific,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Leu,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Ser,
http://linkedlifedata.com/resource/pubmed/chemical/RanGAP1 protein, Xenopus,
http://linkedlifedata.com/resource/pubmed/chemical/XPOT protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/beta Karyopherins,
http://linkedlifedata.com/resource/pubmed/chemical/ran GTP-Binding Protein,
http://linkedlifedata.com/resource/pubmed/chemical/ran-binding protein 1,
http://linkedlifedata.com/resource/pubmed/chemical/tRNA, selenocysteine-
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
359-69
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9660920-Amino Acid Sequence,
pubmed-meshheading:9660920-Animals,
pubmed-meshheading:9660920-Carrier Proteins,
pubmed-meshheading:9660920-Cell Nucleus,
pubmed-meshheading:9660920-Cloning, Molecular,
pubmed-meshheading:9660920-Cytoplasm,
pubmed-meshheading:9660920-GTP-Binding Proteins,
pubmed-meshheading:9660920-GTPase-Activating Proteins,
pubmed-meshheading:9660920-HeLa Cells,
pubmed-meshheading:9660920-Humans,
pubmed-meshheading:9660920-Molecular Sequence Data,
pubmed-meshheading:9660920-Nuclear Proteins,
pubmed-meshheading:9660920-Nucleocytoplasmic Transport Proteins,
pubmed-meshheading:9660920-Oocytes,
pubmed-meshheading:9660920-Protein Binding,
pubmed-meshheading:9660920-RNA, Messenger,
pubmed-meshheading:9660920-RNA, Transfer,
pubmed-meshheading:9660920-RNA, Transfer, Amino Acid-Specific,
pubmed-meshheading:9660920-RNA, Transfer, Leu,
pubmed-meshheading:9660920-RNA, Transfer, Ser,
pubmed-meshheading:9660920-Xenopus,
pubmed-meshheading:9660920-Xenopus Proteins,
pubmed-meshheading:9660920-beta Karyopherins,
pubmed-meshheading:9660920-ran GTP-Binding Protein
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pubmed:year |
1998
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pubmed:articleTitle |
Identification of a tRNA-specific nuclear export receptor.
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pubmed:affiliation |
Zentrum für Molekulare Biologie, Universität Heidelberg, Federal Republic of Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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