ArticleNucleic acids research2013
The role of the C-terminal helix of U1A protein in the interaction with U1hpII RNA.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- NCBP3: A Multifaceted Adaptive Regulator of Gene Expression.Trends in biochemical sciences · 2021Review
- Approaches for measuring the dynamics of RNA-protein interactions.Wiley interdisciplinary reviews. RNA · 2020Review
- Coronavirus genomic RNA packaging.Virology · 2019Review
- Interpreting the Dynamics of Binding Interactions of snRNA and U1A Using a Coarse-Grained Model.Biophysical journal · 2019Article
- Spliceosomal protein U1A is involved in alternative splicing and salt stress tolerance in Arabidopsis thaliana.Nucleic acids research · 2018Article
- Article
- Role of Electrostatics in Protein-RNA Binding: The Global vs the Local Energy Landscape.The journal of physical chemistry. B · 2017Article
- hLARP7 C-terminal domain contains an xRRM that binds the 3' hairpin of 7SK RNA.Nucleic acids research · 2016Article
- An Evolved RNA Recognition Motif That Suppresses HIV-1 Tat/TAR-Dependent Transcription.ACS chemical biology · 2016Article
- Synthetic RNA recognition motifs that selectively recognize HIV-1 trans-activation response element hairpin RNA.ACS chemical biology · 2014Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Previous kinetic investigations of the N-terminal RNA Recognition Motif (RRM) domain of spliceosomal A protein of the U1 small nuclear ribonucleoprotein particle (U1A) interacting with its RNA target U1 hairpin II (U1hpII) provided experimental evidence for a 'lure and lock' model of binding. The final step of locking has been proposed to involve conformational changes in an α-helix immediately C-terminal to the RRM domain (helix C), which occludes the RNA binding surface in the unbound protein. Helix C must shift its position to accommodate RNA binding in the RNA-protein complex. This results in a new hydrophobic core, an intraprotein hydrogen bond and a quadruple stacking interaction between U1A and U1hpII. Here, we used a surface plasmon resonance-based biosensor to gain mechanistic insight into the role of helix C in mediating the interaction with U1hpII. Truncation, removal or disruption of the helix exposes the RNA-binding surface, resulting in an increase in the association rate, while simultaneously reducing the ability of the complex to lock, reflected in a loss of complex stability. Disruption of the quadruple stacking interaction has minor kinetic effects when compared with removal of the intraprotein hydrogen bonds. These data provide new insights into the mechanism whereby sequences C-terminal to an RRM can influence RNA binding.
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