Abstract
Polyglutamine tract-binding protein 1 (PQBP1) is an intrinsically disordered protein composed of a small folded WW domain and a long disordered region. PQBP1 binds to spliceosomal proteins WBP11 and U5-15kD through its N-terminal WW domain and C-terminal region, respectively. Here, we reveal that the binding between PQBP1 and WBP11 reduces the binding affinity between PQBP1 and U5-15kD. Our results suggest that the interaction between PQBP1 and WBP11 negatively modulates the U5-15kD binding of PQBP1 by an allosteric mechanism.
Keywords:
allosteric mechanism; interaction; intrinsically disordered protein.
© 2016 Federation of European Biochemical Societies.
MeSH terms
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Allosteric Regulation / physiology
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Carrier Proteins / chemistry*
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Carrier Proteins / genetics
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Carrier Proteins / metabolism
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DNA-Binding Proteins / chemistry
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism
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Humans
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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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Protein Binding / physiology
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Protein Domains
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RNA Splicing Factors
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Ribonucleoprotein, U5 Small Nuclear / chemistry*
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Ribonucleoprotein, U5 Small Nuclear / genetics
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Ribonucleoprotein, U5 Small Nuclear / metabolism
Substances
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Carrier Proteins
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DNA-Binding Proteins
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Nuclear Proteins
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PQBP1 protein, human
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RNA Splicing Factors
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Ribonucleoprotein, U5 Small Nuclear
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TXNL4A protein, human
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WBP11 protein, human