ArticleNucleic acids research2011
The highly conserved eukaryotic DRG factors are required for efficient translation in a manner redundant with the putative RNA helicase Slh1.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 40 citations in OpenAlex.
- Article
- A spatial long-read approach at near-single-cell resolution reveals developmental regulation of splicing and polyadenylation sites in distinct cortical layers and cell types.Nature communications · 2025Article
- Annotation and functional prediction of RNA helicases inIMA fungus · 2025Review
- Substrate selectivity and inhibition of the human lysyl hydroxylase JMJD7.Protein science : a publication of the Protein Society · 2024Article
- Emerging Role of GCN1 in Disease and Homeostasis.International journal of molecular sciences · 2024Review
- Structure and function of cancer-related developmentally regulated GTP-binding protein 1 (DRG1) is conserved between sponges and humans.Scientific reports · 2022Article
- Conservation of the unusual dimeric JmjC fold of JMJD7 from Drosophila melanogaster to humans.Scientific reports · 2022Article
- Developmentally regulated GTPases: structure, function and roles in disease.Cellular and molecular life sciences : CMLS · 2021Review
- Conserved heterodimeric GTPase Rbg1/Tma46 promotes efficient translation in eukaryotic cells.Cell reports · 2021Article
- Ubiquitin and Ubiquitin-Like Proteins and Domains in Ribosome Production and Function: Chance or Necessity?International journal of molecular sciences · 2021Review
- Structure of Gcn1 bound to stalled and colliding 80S ribosomes.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Ribo-Seq and RNA-Seq ofF1000Research · 2021Article
- The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases.Nature chemical biology · 2018Article
- Developmentally Regulated GTP binding protein 1 (DRG1) controls microtubule dynamics.Scientific reports · 2017Article
- Asc1, Hel2, and Slh1 couple translation arrest to nascent chain degradation.RNA (New York, N.Y.) · 2017Article
- Elevated ZC3H15 increases HCC growth and predicts poor survival after surgical resection.Oncotarget · 2016Article
- RNA helicase proteins as chaperones and remodelers.Annual review of biochemistry · 2014Review
- Interactions between peptidyl tRNA hydrolase homologs and the ribosomal release factor Mrf1 in S. pombe mitochondria.Mitochondrion · 2013Article
- Rbg1-Tma46 dimer structure reveals new functional domains and their role in polysome recruitment.Nucleic acids research · 2012Article
- Review
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eukaryotic and archaeal DRG factors are highly conserved proteins with characteristic GTPase motifs. This suggests their implication in a central biological process, which has so far escaped detection. We show here that the two Saccharomyces cerevisiae DRGs form distinct complexes, RBG1 and RBG2, and that the former co-fractionate with translating ribosomes. A genetic screen for triple synthetic interaction demonstrates that yeast DRGs have redundant function with Slh1, a putative RNA helicase also associating with translating ribosomes. Translation and cell growth are severely impaired in a triple mutant lacking both yeast DRGs and Slh1, but not in double mutants. This new genetic assay allowed us to characterize the roles of conserved motifs present in these proteins for efficient translation and/or association with ribosomes. Altogether, our results demonstrate for the first time a direct role of the highly conserved DRG factors in translation and indicate that this function is redundantly shared by three factors. Furthermore, our data suggest that important cellular processes are highly buffered against external perturbation and, consequently, that redundantly acting factors may escape detection in current high-throughput binary genetic interaction screens.
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