ArticleThe Journal of biological chemistry2013
Small-angle X-ray solution scattering study of the multi-aminoacyl-tRNA synthetase complex reveals an elongated and multi-armed particle.
Article in The Journal of biological chemistry, 2013. 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.
- Case Report: Primed dendritic cell immunotherapy for multiple solid tumors.Frontiers in immunology · 2026Article
- Regulation of BRCA1 stability through the tandem UBX domains of isoleucyl-tRNA synthetase 1.Nature communications · 2022Article
- Human lysyl-tRNA synthetase evolves a dynamic structure that can be stabilized by forming complex.Cellular and molecular life sciences : CMLS · 2022Article
- Structure and Dynamics of the Human Multi-tRNA Synthetase Complex.Sub-cellular biochemistry · 2022Article
- Origin of Proteolytic Stability of Peptide-Brush Polymers as Globular Proteomimetics.ACS central science · 2021Article
- Structural basis for the dynamics of human methionyl-tRNA synthetase in multi-tRNA synthetase complexes.Nucleic acids research · 2021Article
- 3-Dimensional architecture of the human multi-tRNA synthetase complex.Nucleic acids research · 2020Article
- Article
- Retractile lysyl-tRNA synthetase-AIMP2 assembly in the human multi-aminoacyl-tRNA synthetase complex.The Journal of biological chemistry · 2019Article
- Structural control of caspase-generated glutamyl-tRNA synthetase by appended noncatalytic WHEP domains.The Journal of biological chemistry · 2018Article
- Identifying direct contacts between protein complex subunits from their conditional dependence in proteomics datasets.PLoS computational biology · 2017Article
- Experimental approaches for investigation of aminoacyl tRNA synthetase phosphorylation.Methods (San Diego, Calif.) · 2017Review
- Identification of protein interfaces within the multi-aminoacyl-tRNA synthetase complex: the case of lysyl-tRNA synthetase and the scaffold protein p38.FEBS open bio · 2016Article
- Assembly of Multi-tRNA Synthetase Complex via Heterotetrameric Glutathione Transferase-homology Domains.The Journal of biological chemistry · 2015Article
- Calpain Cleaves Most Components in the Multiple Aminoacyl-tRNA Synthetase Complex and Affects Their Functions.The Journal of biological chemistry · 2015Article
- Organization of the multiaminoacyl-tRNA synthetase complex and the cotranslational protein folding.Protein science : a publication of the Protein Society · 2015Article
- Aminoacyl-tRNA synthetase complexes in evolution.International journal of molecular sciences · 2015Review
- Article
- Progress and outlook in structural biology of large viral RNAs.Virus research · 2014Review
- Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In animal cells, nine aminoacyl-tRNA synthetases are associated with the three auxiliary proteins p18, p38, and p43 to form a stable and conserved large multi-aminoacyl-tRNA synthetase complex (MARS), whose molecular mass has been proposed to be between 1.0 and 1.5 MDa. The complex acts as a molecular hub for coordinating protein synthesis and diverse regulatory signal pathways. Electron microscopy studies defined its low resolution molecular envelope as an overall rather compact, asymmetric triangular shape. Here, we have analyzed the composition and homogeneity of the native mammalian MARS isolated from rabbit liver and characterized its overall internal structure, size, and shape at low resolution by hydrodynamic methods and small-angle x-ray scattering in solution. Our data reveal that the MARS exhibits a much more elongated and multi-armed shape than expected from previous reports. The hydrodynamic and structural features of the MARS are large compared with other supramolecular assemblies involved in translation, including ribosome. The large dimensions and non-compact structural organization of MARS favor a large protein surface accessibility for all its components. This may be essential to allow structural rearrangements between the catalytic and cis-acting tRNA binding domains of the synthetases required for binding the bulky tRNA substrates. This non-compact architecture may also contribute to the spatiotemporal controlled release of some of its components, which participate in non-canonical functions after dissociation from the complex.
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