Abstract
The association between Mtr2 and Mex67 is essential for the nuclear export of bulk messenger RNA in yeast. In metazoans, the analogous function is carried out by the TAP-p15 heterodimer. Whereas Mex67 and TAP are highly conserved proteins, their binding partners, Mtr2 and p15, share no sequence similarity, but are nevertheless functionally homologous. Here, we report the 2.8-A resolution crystal structure of Mtr2 in complex with the NTF2-like domain of Mex67. Mtr2 is a novel member of the NTF2-like family and interacts with Mex67, forming a complex with a similar structural architecture to that of TAP-p15. Mtr2 fulfils an analogous function to that of human p15 in maintaining the structural integrity of the heterodimer. In addition, Mtr2 presents a long internal loop, which contains residues that affect the export of the large ribosomal subunit.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Carrier Proteins / chemistry*
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Crystallography, X-Ray
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Dimerization
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Membrane Transport Proteins / chemistry*
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Membrane Transport Proteins / metabolism
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Models, Molecular
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Molecular Sequence Data
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Nuclear Proteins / chemistry
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Nuclear Proteins / metabolism
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Nucleocytoplasmic Transport Proteins / chemistry
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Nucleocytoplasmic Transport Proteins / metabolism
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Protein Binding
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Protein Conformation
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RNA Transport*
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RNA, Messenger / genetics
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RNA, Messenger / metabolism
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RNA-Binding Proteins / chemistry
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RNA-Binding Proteins / metabolism
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Saccharomyces cerevisiae Proteins / chemistry*
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Saccharomyces cerevisiae Proteins / metabolism
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Sequence Homology
Substances
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Carrier Proteins
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MEX67 protein, S cerevisiae
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Membrane Transport Proteins
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Mtr2 protein, S cerevisiae
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Nuclear Proteins
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Nucleocytoplasmic Transport Proteins
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Nutf2 protein, mouse
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Nxt1 protein, mouse
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RNA, Messenger
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RNA-Binding Proteins
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Saccharomyces cerevisiae Proteins