ArticleNucleic acids research2012
Rbg1-Tma46 dimer structure reveals new functional domains and their role in polysome recruitment.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 31 citations in OpenAlex.
- Molecular role of developmentally regulated GTP-binding protein 1 in coordinating osteoclast and osteoblast differentiation during bone remodeling.Molecules and cells · 2026Article
- Phylogenetic and Structural Insights into Melatonin Receptors in Plants: Case Study inPlants (Basel, Switzerland) · 2025Article
- 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
- Review
- Structure of Gcn1 bound to stalled and colliding 80S ribosomes.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Developmentally regulated GTP-binding protein 1 modulates ciliogenesis via an interaction with Dishevelled.The Journal of cell biology · 2019Article
- Druggable Targets in Cyclic Nucleotide Signaling Pathways in Apicomplexan Parasites and Kinetoplastids against Disabling Protozoan Diseases in Humans.International journal of molecular sciences · 2019Review
- 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
- Post-Translational Dosage Compensation Buffers Genetic Perturbations to Stoichiometry of Protein Complexes.PLoS genetics · 2017Article
- The Genomes of Three Uneven Siblings: Footprints of the Lifestyles of Three Trichoderma Species.Microbiology and molecular biology reviews : MMBR · 2016Review
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Developmentally Regulated GTP-binding (DRG) proteins are highly conserved GTPases that associate with DRG Family Regulatory Proteins (DFRP). The resulting complexes have recently been shown to participate in eukaryotic translation. The structure of the Rbg1 GTPase, a yeast DRG protein, in complex with the C-terminal region of its DFRP partner, Tma46, was solved by X-ray diffraction. These data reveal that DRG proteins are multimodular factors with three additional domains, helix-turn-helix (HTH), S5D2L and TGS, packing against the GTPase platform. Surprisingly, the S5D2L domain is inserted in the middle of the GTPase sequence. In contrast, the region of Tma46 interacting with Rbg1 adopts an extended conformation typical of intrinsically unstructured proteins and contacts the GTPase and TGS domains. Functional analyses demonstrate that the various domains of Rbg1, as well as Tma46, modulate the GTPase activity of Rbg1 and contribute to the function of these proteins in vivo. Dissecting the role of the different domains revealed that the Rbg1 TGS domain is essential for the recruitment of this factor in polysomes, supporting further the implication of these conserved factors in translation.
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