Abstract
It is not known how Mex67p and Mtr2p, which form a heterodimer essential for mRNA export, transport mRNPs through the nuclear pore. Here, we show that the Mex67p/Mtr2p complex binds to all of the repeat types (GLFG, FXFG, and FG) found in nucleoporins. For this interaction, complex formation between Mex67p and Mtr2p has to occur. MEX67 and MTR2 also genetically interact with different types of repeat nucleoporins, such as Nup116p, Nup159p, Nsp1p, and Rip1p/Nup40p. These data suggest a model in which nuclear mRNA export requires the Mex67p/Mtr2p heterodimeric complex to directly contact several repeat nucleoporins, organized in different nuclear pore complex subcomplexes, as it carries the mRNP cargo through the nuclear pore.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites
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Cell Nucleus / metabolism*
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Cloning, Molecular
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Crosses, Genetic
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Dimerization
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Fungal Proteins / chemistry
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Fungal Proteins / genetics
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Fungal Proteins / metabolism*
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Nuclear Envelope / metabolism
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Nuclear Proteins / chemistry
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism*
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Nucleocytoplasmic Transport Proteins*
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RNA, Messenger / metabolism*
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RNA-Binding Proteins / chemistry
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RNA-Binding Proteins / genetics
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RNA-Binding Proteins / metabolism*
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Recombinant Fusion Proteins / metabolism
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Recombinant Proteins / metabolism
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / growth & development
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Saccharomyces cerevisiae / physiology*
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Saccharomyces cerevisiae Proteins*
Substances
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Fungal Proteins
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MEX67 protein, S cerevisiae
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Nuclear Proteins
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Nucleocytoplasmic Transport Proteins
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RNA, Messenger
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RNA-Binding Proteins
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Recombinant Fusion Proteins
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Recombinant Proteins
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Saccharomyces cerevisiae Proteins