ArticleNucleic acids research2024
Structure and RNA-binding of the helically extended Roquin CCCH-type zinc finger.
Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- ZFP36 Family Proteins as Critical Regulators of Inflammation, Immune Cell Development, and Antiviral Responses.Vaccines · 2026Review
- RNA-binding proteins and ribonucleoproteins as determinants of immunity.Nature reviews. Immunology · 2026Review
- Evolution of the RNA alternative decayRNA biology · 2025Article
- diPaRIS: Dynamic and Interpretable Protein-RNA Interactions Prediction With U-Shaped Network and Novel Structure Encoding.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- The WRC domain of GRF transcription factors: Structure and DNA recognition.Protein science : a publication of the Protein Society · 2025Article
- Roquin exhibits opposing effects on RNA stem-loop stability through its two ROQ domain binding sites.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Comparative Genomic Analysis Reveals Key Changes in the Genome ofInternational journal of molecular sciences · 2024Article
- Comprehensive Profiling of Roquin Binding Preferences for RNA Stem-Loops.Angewandte Chemie (International ed. in English) · 2024Article
- The role of structure in regulatory RNA elements.Bioscience reports · 2024Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Zinc finger (ZnF) domains appear in a pool of structural contexts and despite their small size achieve varying target specificities, covering single-stranded and double-stranded DNA and RNA as well as proteins. Combined with other RNA-binding domains, ZnFs enhance affinity and specificity of RNA-binding proteins (RBPs). The ZnF-containing immunoregulatory RBP Roquin initiates mRNA decay, thereby controlling the adaptive immune system. Its unique ROQ domain shape-specifically recognizes stem-looped cis-elements in mRNA 3'-untranslated regions (UTR). The N-terminus of Roquin contains a RING domain for protein-protein interactions and a ZnF, which was suggested to play an essential role in RNA decay by Roquin. The ZnF domain boundaries, its RNA motif preference and its interplay with the ROQ domain have remained elusive, also driven by the lack of high-resolution data of the challenging protein. We provide the solution structure of the Roquin-1 ZnF and use an RBNS-NMR pipeline to show that the ZnF recognizes AU-rich RNAs. We systematically refine the contributions of adenines in a poly(U)-background to specific complex formation. With the simultaneous binding of ROQ and ZnF to a natural target transcript of Roquin, our study for the first time suggests how Roquin integrates RNA shape and sequence features through the ROQ-ZnF tandem.
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