ArticleNucleic acids research2005
Kinetic analysis of the role of the tyrosine 13, phenylalanine 56 and glutamine 54 network in the U1A/U1 hairpin II interaction.
Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 35 citations in OpenAlex.
- Spliceosomal SL1 RNA binding to U1-70K: the role of the extended RRM.Nucleic acids research · 2022Article
- Obtaining Crystals of Nucleic Acids in Complex with the Protein U1A Using the Soaking Method.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Fungal biofilm morphology impacts hypoxia fitness and disease progression.Nature microbiology · 2019Article
- Interpreting the Dynamics of Binding Interactions of snRNA and U1A Using a Coarse-Grained Model.Biophysical journal · 2019Article
- The surveillance of pre-mRNA splicing is an early step inGenes & development · 2018Article
- Role of Electrostatics in Protein-RNA Binding: The Global vs the Local Energy Landscape.The journal of physical chemistry. B · 2017Article
- An Evolved RNA Recognition Motif That Suppresses HIV-1 Tat/TAR-Dependent Transcription.ACS chemical biology · 2016Article
- Article
- A compare-and-contrast NMR dynamics study of two related RRMs: U1A and SNF.Biophysical journal · 2014Article
- Synthetic RNA recognition motifs that selectively recognize HIV-1 trans-activation response element hairpin RNA.ACS chemical biology · 2014Article
- Binding affinity and cooperativity control U2B″/snRNA/U2A' RNP formation.Biochemistry · 2014Article
- The role of the C-terminal helix of U1A protein in the interaction with U1hpII RNA.Nucleic acids research · 2013Article
- U1A protein-stem loop 2 RNA recognition: prediction of structural differences from protein mutations.Biopolymers · 2011Article
- Cell-free selection of RNA-binding proteins using in vitro compartmentalization.Nucleic acids research · 2008Article
- Transition state for protein-DNA recognition.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Conformationally restricted nucleotides as a probe of structure-function relationships in RNA.RNA (New York, N.Y.) · 2008Article
- Prediction of salt and mutational effects on the association rate of U1A protein and U1 small nuclear RNA stem/loop II.The journal of physical chemistry. B · 2008Article
- Recognition of essential purines by the U1A protein.BMC biochemistry · 2007Article
- Affinity and specificity of protein U1A-RNA complex formation based on an additive component free energy model.Journal of molecular biology · 2007Article
- A study of collective atomic fluctuations and cooperativity in the U1A-RNA complex based on molecular dynamics simulations.Journal of structural biology · 2007Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The A protein of the U1 small nuclear ribonucleoprotein particle, interacting with its stem-loop RNA target (U1hpII), is frequently used as a paradigm for RNA binding by recognition motif domains (RRMs). U1A/U1hpII complex formation has been proposed to consist of at least two steps: electrostatically mediated alignment of both molecules followed by locking into place, based on the establishment of close-range interactions. The sequence of events between alignment and locking remains obscure. Here we examine the roles of three critical residues, Tyr13, Phe56 and Gln54, in complex formation and stability using Biacore. Our mutational and kinetic data suggest that Tyr13 plays a more important role than Phe56 in complex formation. Mutational analysis of Gln54, combined with molecular dynamics studies, points to Arg52 as another key residue in association. Based on our data and previous structural and modeling studies, we propose that electrostatic alignment of the molecules is followed by hydrogen bond formation between the RNA and Arg52, and the sequential establishment of interactions with loop bases (including Tyr13). A quadruple stack, sandwiching two bases between Phe56 and Asp92, would occur last and coincide with the rearrangement of a C-terminal helix that partially occludes the RRM surface in the free protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.