Assembly of the novel five-component apicomplexan multi-aminoacyl-tRNA synthetase complex is driven by the hybrid scaffold protein Tg-p43.

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-...

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Autores principales:	Jason M van Rooyen, Jean-Benjamin Murat, Pierre-Mehdi Hammoudi, Sylvie Kieffer-Jaquinod, Yohann Coute, Amit Sharma, Hervé Pelloux, Hassan Belrhali, Mohamed-Ali Hakimi
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/0a7c4c4754984a868197eb63a681ace9
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spelling	oai:doaj.org-article:0a7c4c4754984a868197eb63a681ace92021-11-18T08:31:40ZAssembly of the novel five-component apicomplexan multi-aminoacyl-tRNA synthetase complex is driven by the hybrid scaffold protein Tg-p43.1932-620310.1371/journal.pone.0089487https://doaj.org/article/0a7c4c4754984a868197eb63a681ace92014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24586818/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203In 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.Jason M van RooyenJean-Benjamin MuratPierre-Mehdi HammoudiSylvie Kieffer-JaquinodYohann CouteAmit SharmaHervé PellouxHassan BelrhaliMohamed-Ali HakimiPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 2, p e89487 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jason M van Rooyen Jean-Benjamin Murat Pierre-Mehdi Hammoudi Sylvie Kieffer-Jaquinod Yohann Coute Amit Sharma Hervé Pelloux Hassan Belrhali Mohamed-Ali Hakimi Assembly of the novel five-component apicomplexan multi-aminoacyl-tRNA synthetase complex is driven by the hybrid scaffold protein Tg-p43.
description	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.
format	article
author	Jason M van Rooyen Jean-Benjamin Murat Pierre-Mehdi Hammoudi Sylvie Kieffer-Jaquinod Yohann Coute Amit Sharma Hervé Pelloux Hassan Belrhali Mohamed-Ali Hakimi
author_facet	Jason M van Rooyen Jean-Benjamin Murat Pierre-Mehdi Hammoudi Sylvie Kieffer-Jaquinod Yohann Coute Amit Sharma Hervé Pelloux Hassan Belrhali Mohamed-Ali Hakimi
author_sort	Jason M van Rooyen
title	Assembly of the novel five-component apicomplexan multi-aminoacyl-tRNA synthetase complex is driven by the hybrid scaffold protein Tg-p43.
title_short	Assembly of the novel five-component apicomplexan multi-aminoacyl-tRNA synthetase complex is driven by the hybrid scaffold protein Tg-p43.
title_full	Assembly of the novel five-component apicomplexan multi-aminoacyl-tRNA synthetase complex is driven by the hybrid scaffold protein Tg-p43.
title_fullStr	Assembly of the novel five-component apicomplexan multi-aminoacyl-tRNA synthetase complex is driven by the hybrid scaffold protein Tg-p43.
title_full_unstemmed	Assembly of the novel five-component apicomplexan multi-aminoacyl-tRNA synthetase complex is driven by the hybrid scaffold protein Tg-p43.
title_sort	assembly of the novel five-component apicomplexan multi-aminoacyl-trna synthetase complex is driven by the hybrid scaffold protein tg-p43.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/0a7c4c4754984a868197eb63a681ace9
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Assembly of the novel five-component apicomplexan multi-aminoacyl-tRNA synthetase complex is driven by the hybrid scaffold protein Tg-p43.

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