ArticleThe EMBO journal1994
NMR studies of U1 snRNA recognition by the N-terminal RNP domain of the human U1A protein.
Article in The EMBO journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 67 citations in OpenAlex.
- Structural basis underlying CAC RNA recognition by the RRM domain of dimeric RNA-binding protein RBPMS.Quarterly reviews of biophysics · 2016Article
- The role of the C-terminal helix of U1A protein in the interaction with U1hpII RNA.Nucleic acids research · 2013Article
- High-resolution crystal structure of human Dim2/TXNL4B.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Independent alignment of RNA for dynamic studies using residual dipolar couplings.Journal of biomolecular NMR · 2012Article
- Quantitative approaches to monitor protein-nucleic acid interactions using fluorescent probes.RNA (New York, N.Y.) · 2011Review
- Bruno protein contains an expanded RNA recognition motif.Biochemistry · 2009Article
- Article
- Overproduction, purification, crystallization and preliminary X-ray diffraction studies of the human spliceosomal protein TXNL4B.Acta crystallographica. Section F, Structural biology and crystallization communications · 2005Article
- Recognition of GU-rich polyadenylation regulatory elements by human CstF-64 protein.The EMBO journal · 2003Article
- Substitution of an essential adenine in the U1A-RNA complex with a non-polar isostere.Nucleic acids research · 2002Article
- Fourteen residues of the U1 snRNP-specific U1A protein are required for homodimerization, cooperative RNA binding, and inhibition of polyadenylation.Molecular and cellular biology · 2000Article
- Target discrimination by RNA-binding proteins: role of the ancillary protein U2A' and a critical leucine residue in differentiating the RNA-binding specificity of spliceosomal proteins U1A and U2B".RNA (New York, N.Y.) · 1998Article
- Binding of the 60-kDa Ro autoantigen to Y RNAs: evidence for recognition in the major groove of a conserved helix.RNA (New York, N.Y.) · 1998Article
- Determination of the NMR structure of the complex between U1A protein and its RNA polyadenylation inhibition element.Journal of biomolecular NMR · 1998Article
- RNA recognition by the joint action of two nucleolin RNA-binding domains: genetic analysis and structural modeling.The EMBO journal · 1997Article
- From genetic to structural characterization of a new class of RNA-binding domain within the SacY/BglG family of antiterminator proteins.The EMBO journal · 1997Article
- Article
- Variant minihelix RNAs reveal sequence-specific recognition of the helical tRNA(Ser) acceptor stem by E.coli seryl-tRNA synthetase.The EMBO journal · 1996Article
- Molecular characterization of the spliceosomal proteins U1A and U2B" from higher plants.The EMBO journal · 1995Article
- Interaction of the sex-lethal RNA binding domains with RNA.The EMBO journal · 1995Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The RNP domain is a very common motif found in hundreds of proteins, including many protein components of the RNA processing machinery. The 70-90 amino acid domain contains two highly conserved stretches of 6-8 amino acids (RNP-1 and RNP-2) in the central strands of a four-stranded antiparallel beta-sheet, packed against two alpha-helices by a conserved hydrophobic core. Using multidimensional heteronuclear NMR, we have mapped intermolecular contacts between the human U1A protein 102 amino acid N-terminal RNP domain and a 31-mer oligonucleotide derived from stem-loop II of U1 snRNA. Chemical shift changes induced on the protein by the RNA define the surface of the beta-sheet as the recognition interface. The reverse face of the protein, with the two alpha-helices, remains exposed to the solvent in the presence of the RNA, and is potentially available for protein-protein contacts in spliceosome assembly or splice site selection. Protein-RNA contacts occur at the single-stranded apical loop of the hairpin, but also in the major groove of the helical stem at neighbouring U.G and U.U non-Watson-Crick base pairs. Examination of a proposed model for the complex in the light of the present results reveals several features of RNA recognition by RNP proteins. The quality of the spectra for this complex of 22 kDa demonstrates the feasibility of NMR investigation of RNA-protein complexes.
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