title: Dynamic Organization of Aminoacyl-tRNA Synthetase Complexes in the Cytoplasm of Human Cells.
abstract: The localization in space and in time of proteins within the cytoplasm of eukaryotic cells is a central question of the cellular compartmentalization of metabolic pathways. The assembly of proteins within stable or transient complexes plays an essential role in this process. Here, we examined the subcellular localization of the multi-aminoacyl-tRNA synthetase complex in human cells. The sequestration of its components within the cytoplasm rests on the presence of the eukaryotic-specific polypeptide extensions that characterize the human enzymes, as compared with their prokaryotic counterparts. The cellular mobility of several synthetases, assessed by measuring fluorescence recovery after photobleaching, suggested that they are not freely diffusible within the cytoplasm. Several of these enzymes, isolated by tandem affinity purification, were copurified with ribosomal proteins and actin. The capacity of aminoacyl-tRNA synthetases to interact with polyribosomes and with the actin cytoskeleton impacts their subcellular localization and mobility. Our observations have conceptual implications for understanding how translation machinery is organized in vivo.
authors.affiliation: Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, 1 Avenue de la Terrasse, 91190 Gif-sur-Yvette, France.
authors.forename: Monika
authors.initials: M
authors.lastname: Kaminska
authors.affiliation: Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, 1 Avenue de la Terrasse, 91190 Gif-sur-Yvette, France; Institute of Molecular Biology and Genetics, 150 Academy Zabolotnogo Street, 03143 Kiev, Ukraine.
authors.forename: Svitlana
authors.initials: S
authors.lastname: Havrylenko
authors.affiliation: Institut de Biochimie et Biophysique Moléculaire et Cellulaire, UMR 8619 CNRS, Université Paris-Sud, 91405 Orsay, France.
authors.forename: Paulette
authors.initials: P
authors.lastname: Decottignies
authors.affiliation: Institut de Biochimie et Biophysique Moléculaire et Cellulaire, UMR 8619 CNRS, Université Paris-Sud, 91405 Orsay, France.
authors.forename: Pierre
authors.initials: P
authors.lastname: Le Maréchal
authors.affiliation: Institute of Molecular Biology and Genetics, 150 Academy Zabolotnogo Street, 03143 Kiev, Ukraine.
authors.forename: Boris
authors.initials: B
authors.lastname: Negrutskii
authors.affiliation: Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, 1 Avenue de la Terrasse, 91190 Gif-sur-Yvette, France. Electronic address: Marc.Mirande@lebs.cnrs-gif.fr.
authors.forename: Marc
authors.initials: M
authors.lastname: Mirande
mesh_terms: D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D009097:Multienzyme Complexes / Q000378:metabolism*; D011132:Polyribosomes / Q000378:metabolism*; D014176:Protein Biosynthesis / Q000502:physiology*; D021381:Protein Transport / Q000502:physiology
chemical_list: D009097:Multienzyme Complexes; D000604:Amino Acyl-tRNA Synthetases