ArticleNucleic acids research2014
Identification of novel non-canonical RNA-binding sites in Gemin5 involved in internal initiation of translation.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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38 citing papers in PubMed, 53 citations in OpenAlex.
- Ins and outs of IRES elements: function and significance.Biochemical Society transactions · 2025Review
- 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
- The SMN-ribosome interplay: a new opportunity for Spinal Muscular Atrophy therapies.Biochemical Society transactions · 2024Review
- In Vivo and In Vitro Characterization of the RNA Binding Capacity of SETD1A (KMT2F).International journal of molecular sciences · 2023Article
- Novel compound heterozygous mutation and phenotype in the tetratricopeptide repeat-like domain of the GEMIN5 gene in two Chinese families.Journal of human genetics · 2023Article
- Article
- 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
- Functional and structural deficiencies of Gemin5 variants associated with neurological disorders.Life science alliance · 2022Article
- Picornavirus translation strategies.FEBS open bio · 2022Review
- 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
- Uncovering targets of the Leader protease: Linking RNA-mediated pathways and antiviral defense.Wiley interdisciplinary reviews. RNA · 2021Review
- RNA-Binding Proteins at the Host-Pathogen Interface Targeting Viral Regulatory Elements.Viruses · 2021Article
- Loss of function mutations in GEMIN5 cause a neurodevelopmental disorder.Nature communications · 2021Article
- Mutation of Gemin5 Causes Defective Hematopoietic Stem/Progenitor Cells Proliferation in Zebrafish Embryonic Hematopoiesis.Frontiers in cell and developmental biology · 2021Article
- RNA-protein coevolution study of Gemin5 uncovers the role of the PXSS motif of RBS1 domain for RNA binding.RNA biology · 2020Article
- Emerging Roles of Gemin5: From snRNPs Assembly to Translation Control.International journal of molecular sciences · 2020Review
- Structural basis for the dimerization of Gemin5 and its role in protein recruitment and translation control.Nucleic acids research · 2020Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribonucleic acid (RNA)-binding proteins are key players of gene expression control. We have shown that Gemin5 interacts with internal ribosome entry site (IRES) elements and modulates initiation of translation. However, little is known about the RNA-binding sites of this protein. Here we show that the C-terminal region of Gemin5 bears two non-canonical bipartite RNA-binding sites, encompassing amino acids 1297-1412 (RBS1) and 1383-1508 (RBS2). While RBS1 exhibits greater affinity for RNA than RBS2, it does not affect IRES-dependent translation in G5-depleted cells. In solution, the RBS1 three-dimensional structure behaves as an ensemble of flexible conformations rather than having a defined tertiary structure. However, expression of the polypeptide G51383-1508, bearing the low RNA-binding affinity RBS2, repressed IRES-dependent translation. A comparison of the RNA-binding capacity and translation control properties of constructs expressed in mammalian cells to that of the Gemin5 proteolysis products observed in infected cells reveals that non-repressive products accumulated during infection while the repressor polypeptide is not stable. Taken together, our results define the low affinity RNA-binding site as the minimal element of the protein being able to repress internal initiation of translation.
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