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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2004-12-2
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pubmed:abstractText |
Nuclear export of mRNA in eukaryotic cells is mediated by soluble transport factors and components of the nuclear pore complex (NPC). The cytoplasmically oriented nuclear pore protein Nup159 plays a critical role in mRNA export through its conserved N-terminal domain (NTD). Here, we report the crystal structure of the Nup159 NTD, refined to 2.5 A. The structure reveals an unusually asymmetric seven-bladed beta-propeller that is structurally conserved throughout eukarya. Using structure-based conservation analysis, we have targeted specific surface residues for mutagenesis. Residue substitutions in a conserved loop of the NTD abolish in vitro binding to Dbp5, a DEAD box helicase required for mRNA export. In vivo, these mutations cause Dbp5 mislocalization and block mRNA export. These findings suggest that the Nup159 NTD functions in mRNA export as a binding platform, tethering shuttling Dbp5 molecules at the nuclear periphery and locally concentrating this mRNA remodeling factor at the cytoplasmic face of the NPC.
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pubmed:grant |
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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/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/DBP5 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/DEAD-box RNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/NUP159 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Pore Complex Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleocytoplasmic Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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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:day |
3
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
749-60
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15574330-Adenosine Triphosphatases,
pubmed-meshheading:15574330-Biological Transport,
pubmed-meshheading:15574330-Cell Nucleus,
pubmed-meshheading:15574330-Chromatography, Gel,
pubmed-meshheading:15574330-Crystallography, X-Ray,
pubmed-meshheading:15574330-Cytoplasm,
pubmed-meshheading:15574330-DEAD-box RNA Helicases,
pubmed-meshheading:15574330-In Situ Hybridization,
pubmed-meshheading:15574330-Mutagenesis, Site-Directed,
pubmed-meshheading:15574330-Mutation,
pubmed-meshheading:15574330-Nuclear Pore,
pubmed-meshheading:15574330-Nuclear Pore Complex Proteins,
pubmed-meshheading:15574330-Nucleocytoplasmic Transport Proteins,
pubmed-meshheading:15574330-Plasmids,
pubmed-meshheading:15574330-Protein Conformation,
pubmed-meshheading:15574330-Protein Structure, Secondary,
pubmed-meshheading:15574330-Protein Structure, Tertiary,
pubmed-meshheading:15574330-RNA, Messenger,
pubmed-meshheading:15574330-RNA Helicases,
pubmed-meshheading:15574330-Recombinant Proteins,
pubmed-meshheading:15574330-Saccharomyces cerevisiae,
pubmed-meshheading:15574330-Saccharomyces cerevisiae Proteins
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pubmed:year |
2004
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pubmed:articleTitle |
The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore.
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pubmed:affiliation |
Division of Cell and Developmental Biology, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California 94720, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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