ArticleInternational journal of molecular sciences2022
The CAR-mRNA Interaction Surface Is a Zipper Extension of the Ribosome A Site.
Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Anticodon nucleotide modifications affect translational tuning by the ribosomal CAR surface.bioRxiv : the preprint server for biology · 2026Article
- Interplay of the ribosome A and CAR sites.NAR genomics and bioinformatics · 2026Article
- GNN Codon Adjacency Tunes Protein Translation.International journal of molecular sciences · 2024Article
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Authors and funding
8 authors.
Funding
Abstract
The ribosome CAR interaction surface behaves as an extension of the decoding center A site and has H-bond interactions with the +1 codon, which is next in line to enter the A site. Through molecular dynamic simulations, we investigated the codon sequence specificity of this CAR-mRNA interaction and discovered a strong preference for GCN codons, suggesting that there may be a sequence-dependent layer of translational regulation dependent on the CAR interaction surface. Dissection of the CAR-mRNA interaction through nucleotide substitution experiments showed that the first nucleotide of the +1 codon dominates over the second nucleotide position, consistent with an energetically favorable zipper-like activity that emanates from the A site through the CAR-mRNA interface. Moreover, the CAR/+1 codon interaction is affected by the identity of nucleotide 3 of +1 GCN codons, which influences the stacking of G and C. Clustering analysis suggests that the A-site decoding center adopts different neighborhood substates that depend on the identity of the +1 codon.
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