ArticlePloS one2014
Assembly of the novel five-component apicomplexan multi-aminoacyl-tRNA synthetase complex is driven by the hybrid scaffold protein Tg-p43.
Article in PloS one, 2014. 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, 25 citations in OpenAlex.
- Human aminoacyl-tRNA synthetases as integrators of translation and cell signalling networks.Nature reviews. Molecular cell biology · 2026Review
- Unexpected enzymatic function of an ancient nucleic acid-binding fold.Nucleic acids research · 2025Article
- Article
- Solution X-ray scattering highlights discrepancies in Plasmodium multi-aminoacyl-tRNA synthetase complexes.Protein science : a publication of the Protein Society · 2023Article
- Discovery of two distinct aminoacyl-tRNA synthetase complexes anchored to the Plasmodium surface tRNA import protein.The Journal of biological chemistry · 2022Article
- Structure and Dynamics of the Human Multi-tRNA Synthetase Complex.Sub-cellular biochemistry · 2022Article
- Structural basis for the dynamics of human methionyl-tRNA synthetase in multi-tRNA synthetase complexes.Nucleic acids research · 2021Article
- Characterization of aeLife · 2018Article
- Protein Translation Enzyme lysyl-tRNA Synthetase Presents a New Target for Drug Development against Causative Agents of Loiasis and Schistosomiasis.PLoS neglected tropical diseases · 2016Article
- Apicomplexa-specific tRip facilitates import of exogenous tRNAs into malaria parasites.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Recent advances in the biology and drug targeting of malaria parasite aminoacyl-tRNA synthetases.Malaria journal · 2016Review
- Aminoacyl-tRNA synthetase complexes in evolution.International journal of molecular sciences · 2015Review
- Novel and unique domains in aminoacyl-tRNA synthetases from human fungal pathogens Aspergillus niger, Candida albicans and Cryptococcus neoformans.BMC genomics · 2014Article
- Structural and functional analysis of the anti-malarial drug target prolyl-tRNA synthetase.Journal of structural and functional genomics · 2014Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Toxoplasma gondii, as in other eukaryotes, a subset of the amino-acyl-tRNA synthetases are arranged into an abundant cytoplasmic multi-aminoacyl-tRNA synthetase (MARS) complex. Through a series of genetic pull-down assays, we have identified the enzymes of this complex as: methionyl-, glutaminyl-, glutamyl-, and tyrosyl-tRNA synthetases, and we show that the N-terminal GST-like domain of a partially disordered hybrid scaffold protein, Tg-p43, is sufficient for assembly of the intact complex. Our gel filtration studies revealed significant heterogeneity in the size and composition of isolated MARS complexes. By targeting the tyrosyl-tRNA synthetases subunit, which was found exclusively in the complete 1 MDa complex, we were able to directly visualize MARS particles in the electron microscope. Image analyses of the negative stain data revealed the observed heterogeneity and instability of these complexes to be driven by the intrinsic flexibility of the domain arrangements within the MARS complex. These studies provide unique insights into the assembly of these ubiquitous but poorly understood eukaryotic complexes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.