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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6598
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pubmed:dateCreated |
1996-10-24
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pubmed:databankReference |
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pubmed:abstractText |
The Rev protein of human immunodeficiency virus type 1 (HIV-1) mediates the translocation of viral messenger RNAs from the nucleus to the cytoplasm. In yeast, Rev can mediate the nuclear export of Rev response-element-containing RNAs. The export of Rev itself proceeds through the nuclear pore complex and requires a nuclear export signal (NES) and interaction with a cellular cofactor, the protein Rip1. Endogenous RNA export mediators that interact with Rip1 and harbour NESs are thought to exist but have yet to be identified. Here we report the characterization of a new and essential yeast protein, Gle1, which contains an NES and has a relative molecular mass of 62,000. Mutation of the NES in Gle1 prevents export of polyadenylated RNA from the nucleus. Gle1 interacts with Rip1 and the nucleoporin Nup100 and is localized predominantly at nuclear pore complexes. These properties indicate that Gle1 is an RNA-export factor and that Rev may mediate viral RNA export by mimicking the function of Gle1.
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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/AGFG1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NUP100 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Pore Complex Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Fungal,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0028-0836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
383
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
357-60
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pubmed:dateRevised |
2010-9-20
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pubmed:meshHeading |
pubmed-meshheading:8848052-Amino Acid Sequence,
pubmed-meshheading:8848052-Base Sequence,
pubmed-meshheading:8848052-Biological Transport,
pubmed-meshheading:8848052-Carrier Proteins,
pubmed-meshheading:8848052-Cell Line,
pubmed-meshheading:8848052-Cell Nucleus,
pubmed-meshheading:8848052-Cloning, Molecular,
pubmed-meshheading:8848052-Fungal Proteins,
pubmed-meshheading:8848052-Humans,
pubmed-meshheading:8848052-Membrane Proteins,
pubmed-meshheading:8848052-Molecular Sequence Data,
pubmed-meshheading:8848052-Mutagenesis, Site-Directed,
pubmed-meshheading:8848052-Nuclear Envelope,
pubmed-meshheading:8848052-Nuclear Pore Complex Proteins,
pubmed-meshheading:8848052-Nuclear Proteins,
pubmed-meshheading:8848052-Oligodeoxyribonucleotides,
pubmed-meshheading:8848052-Protein Sorting Signals,
pubmed-meshheading:8848052-RNA, Fungal,
pubmed-meshheading:8848052-RNA, Messenger,
pubmed-meshheading:8848052-RNA-Binding Proteins,
pubmed-meshheading:8848052-Saccharomyces cerevisiae,
pubmed-meshheading:8848052-Saccharomyces cerevisiae Proteins
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pubmed:year |
1996
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pubmed:articleTitle |
An RNA-export mediator with an essential nuclear export signal.
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pubmed:affiliation |
Department of Cell Biology and Physiology, Washington University School of Medicine, St Louis, Missouri 63110, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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