RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins.
An RNA recognition motif (RRM) of approximately 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 U1 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 beta-strands and two alpha-helices. The highly conserved RNP1 and RNP2 consensus sequences, containing residues previously suggested to be involved in nucleic acid binding, are juxtaposed in adjacent beta-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.
Duke Scholars
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- Sequence Homology, Nucleic Acid
- Ribosomal Proteins
- Ribonucleoproteins, Small Nuclear
- Ribonucleoproteins
- Recombinant Proteins
- RNA, Small Nuclear
- Protein Conformation
- Molecular Sequence Data
- Models, Molecular
- Magnetic Resonance Spectroscopy
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Sequence Homology, Nucleic Acid
- Ribosomal Proteins
- Ribonucleoproteins, Small Nuclear
- Ribonucleoproteins
- Recombinant Proteins
- RNA, Small Nuclear
- Protein Conformation
- Molecular Sequence Data
- Models, Molecular
- Magnetic Resonance Spectroscopy