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

Research output: Contribution to journalArticle

161 Scopus citations

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
DOIs
StatePublished - Jan 1 1991
Externally publishedYes

Keywords

  • NMR structure
  • RNA recognition motif
  • Ribonucleoprotein consensus sequence

ASJC Scopus subject areas

  • General

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