RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins

David W. Hoffman, Charles C. Query, Barbara L. Golden, Stephen W. White, Jack D. Keene

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158 Citations (Scopus)

Abstract

An RNA recognition motif (RRM) of ≈80 amino acids constitutes the core of RNA-binding domains found in a large family of proteins involved in RNA processing. The U1 RNA-binding domain of the A protein component of the human III small nuclear ribonucleoprotein (RNP), which encompasses the RRM sequence, was analyzed by using NMR spectroscopy. The domain of the A protein is a highly stable monomer in solution consisting of four antiparallel β-strands and two α-helices. The highly conserved RNP1 and RNP2 consensus sequences, containing residues previously suggested to be involved in nucleic acid binding, are juxtaposed in adjacent β-strands. Conserved aromatic side chains that are critical for RNA binding are clustered on the surface of the molecule adjacent to a variable loop that influences recognition of specific RNA sequences. The secondary structure and topology of the RRM are similar to those of ribosomal proteins L12 and L30, suggesting a distant evolutionary relationship between these two types of RNA-associated proteins.

Original languageEnglish (US)
Pages (from-to)2495-2499
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume88
Issue number6
StatePublished - 1991
Externally publishedYes

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U1 Small Nuclear Ribonucleoproteins
Ribosomal Proteins
Magnetic Resonance Spectroscopy
RNA
Small Nuclear Ribonucleoproteins
Consensus Sequence
Nucleic Acids
Proteins
Amino Acids
RNA Recognition Motif Proteins
RNA Recognition Motif

Keywords

  • NMR structure
  • Ribonucleoprotein consensus sequence
  • RNA recognition motif

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

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title = "RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins",
abstract = "An RNA recognition motif (RRM) of ≈80 amino acids constitutes the core of RNA-binding domains found in a large family of proteins involved in RNA processing. The U1 RNA-binding domain of the A protein component of the human III small nuclear ribonucleoprotein (RNP), which encompasses the RRM sequence, was analyzed by using NMR spectroscopy. The domain of the A protein is a highly stable monomer in solution consisting of four antiparallel β-strands and two α-helices. The highly conserved RNP1 and RNP2 consensus sequences, containing residues previously suggested to be involved in nucleic acid binding, are juxtaposed in adjacent β-strands. Conserved aromatic side chains that are critical for RNA binding are clustered on the surface of the molecule adjacent to a variable loop that influences recognition of specific RNA sequences. The secondary structure and topology of the RRM are similar to those of ribosomal proteins L12 and L30, suggesting a distant evolutionary relationship between these two types of RNA-associated proteins.",
keywords = "NMR structure, Ribonucleoprotein consensus sequence, RNA recognition motif",
author = "Hoffman, {David W.} and Query, {Charles C.} and Golden, {Barbara L.} and White, {Stephen W.} and Keene, {Jack D.}",
year = "1991",
language = "English (US)",
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pages = "2495--2499",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
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TY - JOUR

T1 - RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins

AU - Hoffman, David W.

AU - Query, Charles C.

AU - Golden, Barbara L.

AU - White, Stephen W.

AU - Keene, Jack D.

PY - 1991

Y1 - 1991

N2 - An RNA recognition motif (RRM) of ≈80 amino acids constitutes the core of RNA-binding domains found in a large family of proteins involved in RNA processing. The U1 RNA-binding domain of the A protein component of the human III small nuclear ribonucleoprotein (RNP), which encompasses the RRM sequence, was analyzed by using NMR spectroscopy. The domain of the A protein is a highly stable monomer in solution consisting of four antiparallel β-strands and two α-helices. The highly conserved RNP1 and RNP2 consensus sequences, containing residues previously suggested to be involved in nucleic acid binding, are juxtaposed in adjacent β-strands. Conserved aromatic side chains that are critical for RNA binding are clustered on the surface of the molecule adjacent to a variable loop that influences recognition of specific RNA sequences. The secondary structure and topology of the RRM are similar to those of ribosomal proteins L12 and L30, suggesting a distant evolutionary relationship between these two types of RNA-associated proteins.

AB - An RNA recognition motif (RRM) of ≈80 amino acids constitutes the core of RNA-binding domains found in a large family of proteins involved in RNA processing. The U1 RNA-binding domain of the A protein component of the human III small nuclear ribonucleoprotein (RNP), which encompasses the RRM sequence, was analyzed by using NMR spectroscopy. The domain of the A protein is a highly stable monomer in solution consisting of four antiparallel β-strands and two α-helices. The highly conserved RNP1 and RNP2 consensus sequences, containing residues previously suggested to be involved in nucleic acid binding, are juxtaposed in adjacent β-strands. Conserved aromatic side chains that are critical for RNA binding are clustered on the surface of the molecule adjacent to a variable loop that influences recognition of specific RNA sequences. The secondary structure and topology of the RRM are similar to those of ribosomal proteins L12 and L30, suggesting a distant evolutionary relationship between these two types of RNA-associated proteins.

KW - NMR structure

KW - Ribonucleoprotein consensus sequence

KW - RNA recognition motif

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ER -