Abstract
Although highly homologous, the spliceosomal hPrp31 and the nucleolar Nop56 and Nop58 (Nop56/58) proteins recognize different ribonucleoprotein (RNP) particles. hPrp31 interacts with complexes containing the 15.5K protein and U4 or U4atac small nuclear RNA (snRNA), whereas Nop56/58 associate with 15.5K-box C/D small nucleolar RNA complexes. We present structural and biochemical analyses of hPrp31-15.5K-U4 snRNA complexes that show how the conserved Nop domain in hPrp31 maintains high RNP binding selectivity despite relaxed RNA sequence requirements. The Nop domain is a genuine RNP binding module, exhibiting RNA and protein binding surfaces. Yeast two-hybrid analyses suggest a link between retinitis pigmentosa and an aberrant hPrp31-hPrp6 interaction that blocks U4/U6-U5 tri-snRNP formation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Motifs
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Amino Acid Sequence
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Amino Acid Substitution
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Carrier Proteins / chemistry
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Carrier Proteins / metabolism
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Eye Proteins / chemistry*
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Eye Proteins / metabolism*
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Humans
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Hydrophobic and Hydrophilic Interactions
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Models, Molecular
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Molecular Sequence Data
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Mutation
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Nucleic Acid Conformation
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Protein Binding
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Protein Conformation
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Protein Structure, Secondary
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Protein Structure, Tertiary
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RNA Splicing Factors
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RNA, Small Nuclear / chemistry*
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RNA, Small Nuclear / metabolism*
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RNA-Binding Proteins
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Retinitis Pigmentosa / genetics
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Ribonucleoprotein, U4-U6 Small Nuclear / chemistry*
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Ribonucleoprotein, U4-U6 Small Nuclear / metabolism*
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Transcription Factors
Substances
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Carrier Proteins
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Eye Proteins
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PRPF31 protein, human
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PRPF6 protein, human
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RNA Splicing Factors
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RNA, Small Nuclear
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RNA-Binding Proteins
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Ribonucleoprotein, U4-U6 Small Nuclear
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Transcription Factors
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U4 small nuclear RNA