ArticleGenes & development2016
Structural basis for snRNA recognition by the double-WD40 repeat domain of Gemin5.
Article in Genes & development, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 56 citations in OpenAlex.
- Proteins that recognize unique features of U7 snRNA and may substitute for Gemin5 in the assembly of U7-specific Sm ring.RNA (New York, N.Y.) · 2025Article
- Developmental and Epileptic Encephalopathy: Pathogenesis of Intellectual Disability Beyond Channelopathies.Biomolecules · 2025Review
- Oligomerization regulates the interaction of Gemin5 with members of the SMN complex and the translation machinery.Cell death discovery · 2024Article
- Expanding the clinical phenotype and genetic spectrum of GEMIN5 disorders: Early-infantile developmental and epileptic encephalopathies.Brain and behavior · 2024Article
- Alternative splicing events driven by altered levels of GEMIN5 undergo translation.RNA biology · 2024Article
- The SMN complex drives structural changes in human snRNAs to enable snRNP assembly.Nature communications · 2023Article
- Mechanism of assembly of snRNP cores assisted by ICln and the SMN complex in fission yeast.iScience · 2023Article
- SMN regulates GEMIN5 expression and acts as a modifier of GEMIN5-mediated neurodegeneration.Acta neuropathologica · 2023Article
- Structural basis for Gemin5 decamer-mediated mRNA binding.Nature communications · 2022Article
- Gemin5-dependent RNA association with polysomes enables selective translation of ribosomal and histone mRNAs.Cellular and molecular life sciences : CMLS · 2022Article
- Molecular insights into RNA recognition and gene regulation by the TRIM-NHL protein Mei-P26.Life science alliance · 2022Article
- Functional and structural deficiencies of Gemin5 variants associated with neurological disorders.Life science alliance · 2022Article
- Transcriptome-Wide Identification of Coding and Noncoding RNA-Binding Proteins Defines the Comprehensive RNA Interactome of Leishmania mexicana.Microbiology spectrum · 2022Article
- Phosphorylation of T897 in the dimerization domain of Gemin5 modulates protein interactions and translation regulation.Computational and structural biotechnology journal · 2022Article
- The RBS1 domain of Gemin5 is intrinsically unstructured and interacts with RNA through conserved Arg and aromatic residues.RNA biology · 2021Article
- The epigenetic factor FVE orchestrates cytoplasmic SGS3-DRB4-DCL4 activities to promote transgene silencing inScience advances · 2021Article
- Identification and structural analysis of the Schizosaccharomyces pombe SMN complex.Nucleic acids research · 2021Article
- Biology of the mRNA Splicing Machinery and Its Dysregulation in Cancer Providing Therapeutic Opportunities.International journal of molecular sciences · 2021Review
- Loss of function mutations in GEMIN5 cause a neurodevelopmental disorder.Nature communications · 2021Article
- DIS3L2 and LSm proteins are involved in the surveillance of Sm ring-deficient snRNAs.Nucleic acids research · 2020Article
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Assembly of the spliceosomal small nuclear ribonucleoparticle (snRNP) core requires the participation of the multisubunit SMN (survival of motor neuron) complex, which contains SMN and several Gemin proteins. The SMN and Gemin2 subunits directly bind Sm proteins, and Gemin5 is required for snRNP biogenesis and has been implicated in snRNA recognition. The RNA sequence required for snRNP assembly includes the Sm site and an adjacent 3' stem-loop, but a precise understanding of Gemin5's RNA-binding specificity is lacking. Here we show that the N-terminal half of Gemin5, which is composed of two juxtaposed seven-bladed WD40 repeat domains, recognizes the Sm site. The tandem WD40 repeat domains are rigidly held together to form a contiguous RNA-binding surface. RNA-contacting residues are located mostly on loops between β strands on the apical surface of the WD40 domains. Structural and biochemical analyses show that base-stacking interactions involving four aromatic residues and hydrogen bonding by a pair of arginines are crucial for specific recognition of the Sm sequence. We also show that an adenine immediately 5' to the Sm site is required for efficient binding and that Gemin5 can bind short RNA oligos in an alternative mode. Our results provide mechanistic understandings of Gemin5's snRNA-binding specificity as well as valuable insights into the molecular mechanism of RNA binding by WD40 repeat proteins in general.
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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.