Discovery of two distinct aminoacyl-tRNA synthetase complexes anchored to the Plasmodium surface tRNA import protein
| Autor: | José R. Jaramillo Ponce, Delphine Kapps, Caroline Paulus, Johana Chicher, Magali Frugier |
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| Přispěvatelé: | Architecture et Réactivité de l'ARN (ARN), Institut de biologie moléculaire et cellulaire (IBMC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg (UNISTRA), univOAK, Archive ouverte |
| Rok vydání: | 2021 |
| Předmět: |
multiaminoacyl-tRNA synthetase complex
Plasmodium berghei RNA-binding protein Protozoan Proteins Methionine-tRNA Ligase Sciences du Vivant [q-bio]/Biochimie Biologie Moléculaire Biochemistry aminoacyl-tRNA synthetase–interacting multifunctional proteins (AIMP) Amino Acyl-tRNA Synthetases RNA Transfer [SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology Humans aminoacyl-tRNA synthetase [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Molecular Biology tRNA protein complex Membrane Proteins Nuclear Proteins RNA-Binding Proteins cell surface protein Cell Biology GST-like domain Neoplasm Proteins Cytokines human activities |
| Zdroj: | Journal of Biological Chemistry Journal of Biological Chemistry, 2022, pp.101987. ⟨10.1016/j.jbc.2022.101987⟩ |
| ISSN: | 1083-351X 0021-9258 |
| DOI: | 10.1016/j.jbc.2022.101987⟩ |
| Popis: | Aminoacyl-tRNA synthetases (aaRSs) attach amino acids to their cognate transfer RNAs. In eukaryotes, a subset of cytosolic aaRSs is organized into a multisynthetase complex (MSC), along with specialized scaffolding proteins referred to as aaRS-interacting multifunctional proteins (AIMPs). In Plasmodium, the causative agent of malaria, the tRNA import protein (tRip), is a membrane protein that participates in tRNA trafficking; we show that tRip also functions as an AIMP. We identified three aaRSs, the glutamyl-tRNA synthetase (ERS), glutaminyl-tRNA synthetase (QRS), and methionyl-tRNA synthetase (MRS), which were specifically coimmunoprecipitated with tRip in Plasmodium berghei blood stage parasites. All four proteins contain an N-terminal glutathione-S-transferase (GST)-like domain that was demonstrated to be involved in MSC assembly. In contrast to previous studies, further dissection of GST-like interactions identified two exclusive heterotrimeric complexes: the Q-complex (tRip-ERS-QRS) and the M-complex (tRip-ERS-MRS). Gel filtration and light scattering suggest a 2:2:2 stoichiometry for both complexes but with distinct biophysical properties and mutational analysis further revealed that the GST-like domains of QRS and MRS use different strategies to bind ERS. Taken together, our results demonstrate that neither the singular homodimerization of tRip nor its localization in the parasite plasma membrane prevents the formation of MSCs in Plasmodium. Besides, the extracellular localization of the tRNA-binding module of tRip is compensated by the presence of additional tRNA-binding modules fused to MRS and QRS, providing each MSC with two spatially distinct functions: aminoacylation of intraparasitic tRNAs and binding of extracellular tRNAs. This unique host-pathogen interaction is discussed. |
| Databáze: | OpenAIRE |
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