Abstract
Variations in a polymorphic (TG)m sequence near exon 9 of the human CFTR gene have been associated with variable proportions of exon skipping and occurrence of disease. We have recently identified nuclear factor TDP-43 as a novel splicing regulator capable of binding to this element in the CFTR pre-mRNA and inhibiting recognition of the neighboring exon. In this study we report the dissection of the RNA binding properties of TDP-43 and their functional implications in relationship with the splicing process. Our results show that this protein contains two fully functional RNA recognition motif (RRM) domains with distinct RNA/DNA binding characteristics. Interestingly, TDP-43 can bind a minimum number of six UG (or TG) single-stranded dinucleotide stretches, and binding affinity increases with the number of repeats. In particular, the highly conserved Phe residues in the first RRM region play a key role in nucleic acid recognition.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alternative Splicing*
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Amino Acid Motifs
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Amino Acid Sequence
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Binding, Competitive
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Cell Nucleus / metabolism*
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Cystic Fibrosis Transmembrane Conductance Regulator / genetics
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Cystic Fibrosis Transmembrane Conductance Regulator / metabolism*
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DNA / metabolism
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DNA-Binding Proteins / chemistry*
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Exons
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Gene Deletion
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Glutathione Transferase / metabolism
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Humans
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Molecular Sequence Data
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Mutation
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Nucleic Acids / metabolism
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Oligonucleotides / metabolism
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Phenylalanine / chemistry
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Plasmids / metabolism
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Polymorphism, Genetic
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Protein Binding
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Protein Structure, Tertiary
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RNA / metabolism
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RNA, Messenger / metabolism
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Recombinant Fusion Proteins / metabolism
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Recombinant Proteins / metabolism
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Sequence Homology, Amino Acid
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Ultraviolet Rays
Substances
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CFTR protein, human
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DNA-Binding Proteins
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Nucleic Acids
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Oligonucleotides
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RNA, Messenger
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Recombinant Fusion Proteins
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Recombinant Proteins
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Cystic Fibrosis Transmembrane Conductance Regulator
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Phenylalanine
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RNA
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DNA
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Glutathione Transferase