ArticleNucleic acids research2014
SAXS analysis of the tRNA-modifying enzyme complex MnmE/MnmG reveals a novel interaction mode and GTP-induced oligomerization.
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 17 papers.
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17 citing papers in PubMed, 31 citations in OpenAlex.
- Cryo-EM structures of the MnmE-MnmG complex reveal large conformational changes and provide new insights into the mechanism of tRNA modification.Nucleic acids research · 2025Article
- 2-Thiouridine formation inJournal of bacteriology · 2025Review
- tRNA modifying enzymes MnmE and MnmG are essential forbioRxiv : the preprint server for biology · 2025Article
- Taurine hypomodification underlies mitochondrial tRNATrp-related genetic diseases.Nucleic acids research · 2024Article
- Insights into the Mechanism of Installation of 5-Carboxymethylaminomethyl Uridine Hypermodification by tRNA-Modifying Enzymes MnmE and MnmG.Journal of the American Chemical Society · 2023Article
- Article
- The human tRNA taurine modification enzyme GTPBP3 is an active GTPase linked to mitochondrial diseases.Nucleic acids research · 2021Article
- Proteomic and Metabolomic Analyses Provide Insights into the Mechanism on Arginine Metabolism Regulated by tRNA Modification Enzymes GidA and MnmE ofFrontiers in cellular and infection microbiology · 2020Article
- Combination of coarse-grained molecular dynamics simulations and small-angle X-ray scattering experiments.Biophysics and physicobiology · 2019Article
- MnmE, a Central tRNA-Modifying GTPase, Is Essential for the Growth, Pathogenicity, and Arginine Metabolism ofFrontiers in cellular and infection microbiology · 2019Article
- Cryo-EM shows stages of initial codon selection on the ribosome by aa-tRNA in ternary complex with GTP and the GTPase-deficient EF-TuH84A.Nucleic acids research · 2018Article
- Structural and biochemical analysis ofThe Journal of biological chemistry · 2017Article
- A Structure-free Method for Quantifying Conformational Flexibility in proteins.Scientific reports · 2016Article
- GidA, a tRNA Modification Enzyme, Contributes to the Growth, and Virulence of Streptococcus suis Serotype 2.Frontiers in cellular and infection microbiology · 2016Article
- pyDockSAXS: protein-protein complex structure by SAXS and computational docking.Nucleic acids research · 2015Article
- Versatile sample environments and automation for biological solution X-ray scattering experiments at the P12 beamline (PETRA III, DESY).Journal of applied crystallography · 2015Article
- Modification of the wobble uridine in bacterial and mitochondrial tRNAs reading NNA/NNG triplets of 2-codon boxes.RNA biology · 2014Review
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transfer ribonucleic acid (tRNA) modifications, especially at the wobble position, are crucial for proper and efficient protein translation. MnmE and MnmG form a protein complex that is implicated in the carboxymethylaminomethyl modification of wobble uridine (cmnm(5)U34) of certain tRNAs. MnmE is a G protein activated by dimerization (GAD), and active guanosine-5'-triphosphate (GTP) hydrolysis is required for the tRNA modification to occur. Although crystal structures of MnmE and MnmG are available, the structure of the MnmE/MnmG complex (MnmEG) and the nature of the nucleotide-induced conformational changes and their relevance for the tRNA modification reaction remain unknown. In this study, we mainly used small-angle X-ray scattering to characterize these conformational changes in solution and to unravel the mode of interaction between MnmE, MnmG and tRNA. In the nucleotide-free state MnmE and MnmG form an unanticipated asymmetric α2β2 complex. Unexpectedly, GTP binding promotes further oligomerization of the MnmEG complex leading to an α4β2 complex. The transition from the α2β2 to the α4β2 complex is fast, reversible and coupled to GTP binding and hydrolysis. We propose a model in which the nucleotide-induced changes in conformation and oligomerization of MnmEG form an integral part of the tRNA modification reaction cycle.
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