Abstract
Mex67p and Mtr2p constitute an essential mRNA export complex that interacts with poly(A)+ RNA and nuclear pore proteins. We have identified Yra1p, an intranuclear protein with in vitro RNA-RNA annealing activity, which directly binds to Mex67p. The complex between Yra1p and Mex67p was reconstituted in vitro and shown by UV-crosslinking to bind directly to RNA. Mutants of YRA1 are impaired in nuclear poly(A)+ RNA export at restrictive growth conditions. ALY, the mouse homologue of Yra1p and a transcriptional coactivator, can bind in vitro to yeast and human Mex67p and partly complements the otherwise non-viable yra1 null mutant. Thus, Yra1p is the first RNA-binding protein characterized, which bridges the shuttling Mex67p/Mtr2p exporter to intranuclear mRNA transport cargoes.
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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Animals
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Biological Transport
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Fungal Proteins / genetics
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Fungal Proteins / metabolism*
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Humans
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Mice
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Microscopy, Fluorescence
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Molecular Sequence Data
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Mutation
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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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Poly A / genetics
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Protein Binding
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RNA, Messenger / metabolism*
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RNA-Binding Proteins / genetics
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RNA-Binding Proteins / metabolism*
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Saccharomyces cerevisiae Proteins*
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Sequence Homology, Amino Acid
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Transcription Factors / metabolism
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Yeasts / genetics
Substances
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ALYREF protein, human
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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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Refbp1 protein, mouse
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Saccharomyces cerevisiae Proteins
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Transcription Factors
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YRA1 protein, S cerevisiae
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Poly A