ArticleNucleic acids research2002
Investigation of a conserved stacking interaction in target site recognition by the U1A protein.
Article in Nucleic acids research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 45 citations in OpenAlex.
- TDP-43 regulates site-specific 2'-O-methylation of U1 and U2 snRNAs via controlling the Cajal body localization of a subset of C/D scaRNAs.Nucleic acids research · 2019Article
- Structural basis for snRNA recognition by the double-WD40 repeat domain of Gemin5.Genes & development · 2016Article
- Topology of RNA-protein nucleobase-amino acid π-π interactions and comparison to analogous DNA-protein π-π contacts.RNA (New York, N.Y.) · 2016Article
- Evolution of the genetic code by incorporation of amino acids that improved or changed protein function.Journal of molecular evolution · 2013Article
- The role of the C-terminal helix of U1A protein in the interaction with U1hpII RNA.Nucleic acids research · 2013Article
- Intrinsic flexibility of snRNA hairpin loops facilitates protein binding.RNA (New York, N.Y.) · 2012Article
- U1A protein-stem loop 2 RNA recognition: prediction of structural differences from protein mutations.Biopolymers · 2011Article
- Crystal structure of a human cleavage factor CFI(m)25/CFI(m)68/RNA complex provides an insight into poly(A) site recognition and RNA looping.Structure (London, England : 1993) · 2011Article
- A simple ligand that selectively targets CUG trinucleotide repeats and inhibits MBNL protein binding.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Adjustable ellipsoid nanoparticles assembled from re-engineered connectors of the bacteriophage phi29 DNA packaging motor.ACS nano · 2009Article
- Cell-free selection of RNA-binding proteins using in vitro compartmentalization.Nucleic acids research · 2008Article
- Prediction of interacting single-stranded RNA bases by protein-binding patterns.Journal of molecular biology · 2008Article
- Characterization of the dynamics of an essential helix in the U1A protein by time-resolved fluorescence measurements.The journal of physical chemistry. B · 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
- Do collective atomic fluctuations account for cooperative effects? Molecular dynamics studies of the U1A-RNA complex.Journal of the American Chemical Society · 2006Article
- A single intermolecular contact mediates intramolecular stabilization of both RNA and protein.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Kinetic analysis of the role of the tyrosine 13, phenylalanine 56 and glutamine 54 network in the U1A/U1 hairpin II interaction.Nucleic acids research · 2005Article
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
Three highly conserved aromatic residues in RNA recognition motifs (RRM) participate in stacking interactions with RNA bases upon binding RNA. We have investigated the contribution of one of these aromatic residues, Phe56, to the complex formed between the N-terminal RRM of the spliceosomal protein U1A and stem-loop 2 of U1 snRNA. Previous work showed that the aromatic group is important for high affinity binding. Here we probe how mutation of Phe56 affects the kinetics of complex dissociation, the strength of the hydrogen bonds formed between U1A and the base that stacks with Phe56 (A6) and specific target site recognition. Substitution of Phe56 with Trp or Tyr increased the rate of dissociation of the complex, consistent with previously reported results. However, substitution of Phe56 with His decreased the rate of complex association, implying a change in the initial formation of the complex. Simultaneous modification of residue 56 and A6 revealed energetic coupling between the aromatic group and the functional groups of A6 that hydrogen bond to U1A. Finally, mutation of Phe56 to Leu reduced the ability of U1A to recognize stem-loop 2 correctly. Taken together, these experiments suggest that Phe56 contributes to binding affinity by stacking with A6 and participating in networks of energetically coupled interactions that enable this conserved aromatic amino acid to play a complex role in target site recognition.
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