ArticleNature2014
Structural basis for the assembly of the Sxl-Unr translation regulatory complex.
Article in Nature, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 119 citations in OpenAlex.
- Decoding RNA-protein interactions using high-throughput methods.RNA biology · 2026Review
- The RNA structural code: orchestrating gene expression and enabling precision therapies.Acta pharmacologica Sinica · 2026Review
- Decoding the interactions and functions of non-coding RNA with artificial intelligence.Nature reviews. Molecular cell biology · 2025Review
- The Rbfox1/LASR complex controls alternative pre-mRNA splicing by recognition of multipart RNA regulatory modules.Genes & development · 2025Article
- Exploring the dynamics of messenger ribonucleoprotein-mediated translation repression.Biochemical Society transactions · 2024Review
- CSDE1: a versatile regulator of gene expression in cancer.NAR cancer · 2024Article
- Analysis of the inter-domain orientation of tandem RRM domains with diverse linkers: connecting experimental with AlphaFold2 predicted models.NAR genomics and bioinformatics · 2024Article
- Intra- and inter-molecular regulation by intrinsically-disordered regions governs PUF protein RNA binding.Nature communications · 2023Article
- Upstream of N-Ras C-terminal cold shock domains mediate poly(A) specificity in a novel RNA recognition mode and bind poly(A) binding protein.Nucleic acids research · 2023Article
- Deciphering the RRM-RNA recognition code: A computational analysis.PLoS computational biology · 2023Article
- Structural insights reveal the specific recognition of meiRNA by the Mei2 protein.Journal of molecular cell biology · 2022Article
- Molecular insights into RNA recognition and gene regulation by the TRIM-NHL protein Mei-P26.Life science alliance · 2022Article
- A working model for condensate RNA-binding proteins as matchmakers for protein complex assembly.RNA (New York, N.Y.) · 2022Review
- Validation and classification of RNA binding proteins identified by mRNA interactome capture.RNA (New York, N.Y.) · 2021Article
- The cooperative binding of TDP-43 to GU-rich RNA repeats antagonizes TDP-43 aggregation.eLife · 2021Article
- Matrix-screening reveals a vast potential for direct protein-protein interactions among RNA binding proteins.Nucleic acids research · 2021Article
- A scaffold lncRNA shapes the mitosis to meiosis switch.Nature communications · 2021Article
- Review
- Structural basis of DNA binding to human YB-1 cold shock domain regulated by phosphorylation.Nucleic acids research · 2020Article
- Pseudo-RNA-Binding Domains Mediate RNA Structure Specificity in Upstream of N-Ras.Cell reports · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Genetic equality between males and females is established by chromosome-wide dosage-compensation mechanisms. In the fruitfly Drosophila melanogaster, the dosage-compensation complex promotes twofold hypertranscription of the single male X-chromosome and is silenced in females by inhibition of the translation of msl2, which codes for the limiting component of the dosage-compensation complex. The female-specific protein Sex-lethal (Sxl) recruits Upstream-of-N-ras (Unr) to the 3' untranslated region of msl2 messenger RNA, preventing the engagement of the small ribosomal subunit. Here we report the 2.8 Å crystal structure, NMR and small-angle X-ray and neutron scattering data of the ternary Sxl-Unr-msl2 ribonucleoprotein complex featuring unprecedented intertwined interactions of two Sxl RNA recognition motifs, a Unr cold-shock domain and RNA. Cooperative complex formation is associated with a 1,000-fold increase of RNA binding affinity for the Unr cold-shock domain and involves novel ternary interactions, as well as non-canonical RNA contacts by the α1 helix of Sxl RNA recognition motif 1. Our results suggest that repression of dosage compensation, necessary for female viability, is triggered by specific, cooperative molecular interactions that lock a ribonucleoprotein switch to regulate translation. The structure serves as a paradigm for how a combination of general and widespread RNA binding domains expands the code for specific single-stranded RNA recognition in the regulation of gene expression.
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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.