Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP

Sunbin Liu; Ping Li; Olexandr Dybkov; Stephanie Nottrott; Klaus Hartmuth; Reinhard Lührmann; Teresa Carlomagno; Markus C Wahl

doi:10.1126/science.1137924

Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP

Sunbin Liu, Ping Li, Olexandr Dybkov, Stephanie Nottrott, Klaus Hartmuth, Reinhard Lührmann, Teresa Carlomagno, Markus C Wahl

Biosciences

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	115-20
Number of pages	6
Journal	Science
Volume	316
Issue number	5821
DOIs	https://doi.org/10.1126/science.1137924
Publication status	Published - 6 Apr 2007

Keywords

Amino Acid Motifs
Amino Acid Sequence
Amino Acid Substitution
Carrier Proteins/chemistry
Eye Proteins/chemistry
Humans
Hydrophobic and Hydrophilic Interactions
Models, Molecular
Molecular Sequence Data
Mutation
Nucleic Acid Conformation
Protein Binding
Protein Conformation
Protein Structure, Secondary
Protein Structure, Tertiary
RNA Splicing Factors
RNA, Small Nuclear/chemistry
RNA-Binding Proteins
Retinitis Pigmentosa/genetics
Ribonucleoprotein, U4-U6 Small Nuclear/chemistry
Transcription Factors

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10.1126/science.1137924

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title = "Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP",

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.",

keywords = "Amino Acid Motifs, Amino Acid Sequence, Amino Acid Substitution, Carrier Proteins/chemistry, Eye Proteins/chemistry, Humans, Hydrophobic and Hydrophilic Interactions, Models, Molecular, Molecular Sequence Data, Mutation, Nucleic Acid Conformation, Protein Binding, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, RNA Splicing Factors, RNA, Small Nuclear/chemistry, RNA-Binding Proteins, Retinitis Pigmentosa/genetics, Ribonucleoprotein, U4-U6 Small Nuclear/chemistry, Transcription Factors",

author = "Sunbin Liu and Ping Li and Olexandr Dybkov and Stephanie Nottrott and Klaus Hartmuth and Reinhard L{\"u}hrmann and Teresa Carlomagno and Wahl, {Markus C}",

year = "2007",

month = apr,

day = "6",

doi = "10.1126/science.1137924",

language = "English",

volume = "316",

pages = "115--20",

journal = "Science",

issn = "0036-8075",

publisher = "American Association for the Advancement of Science",

number = "5821",

}

TY - JOUR

T1 - Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP

AU - Liu, Sunbin

AU - Li, Ping

AU - Dybkov, Olexandr

AU - Nottrott, Stephanie

AU - Hartmuth, Klaus

AU - Lührmann, Reinhard

AU - Carlomagno, Teresa

AU - Wahl, Markus C

PY - 2007/4/6

Y1 - 2007/4/6

N2 - 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.

AB - 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.

KW - Amino Acid Motifs

KW - Amino Acid Sequence

KW - Amino Acid Substitution

KW - Carrier Proteins/chemistry

KW - Eye Proteins/chemistry

KW - Humans

KW - Hydrophobic and Hydrophilic Interactions

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Mutation

KW - Nucleic Acid Conformation

KW - Protein Binding

KW - Protein Conformation

KW - Protein Structure, Secondary

KW - Protein Structure, Tertiary

KW - RNA Splicing Factors

KW - RNA, Small Nuclear/chemistry

KW - RNA-Binding Proteins

KW - Retinitis Pigmentosa/genetics

KW - Ribonucleoprotein, U4-U6 Small Nuclear/chemistry

KW - Transcription Factors

U2 - 10.1126/science.1137924

DO - 10.1126/science.1137924

M3 - Article

C2 - 17412961

SN - 0036-8075

VL - 316

SP - 115

EP - 120

JO - Science

JF - Science

IS - 5821

ER -

Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP

Abstract

Keywords

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