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FEBS Lett. 2010 Sep 24;584(18):3842-9. doi: 10.1016/j.febslet.2010.08.023. Epub 2010 Aug 20.

Building arks for tRNA: structure and function of the Arc1p family of non-catalytic tRNA-binding proteins.

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  • 1Laboratory of Biochemistry, School of Medicine, University of Thessaly, BIOPOLIS, Larissa, Greece.


Following the intricate architecture of the eukaryotic cell, protein synthesis involves formation of many macromolecular assemblies, some of which are composed by tRNA-aminoacylation enzymes. Protein-protein and protein-tRNA interactions in these complexes can be facilitated by non-catalytic tRNA-binding proteins. This review focuses on the dissection of the molecular, structural and functional properties of a particular family of such proteins: yeast Arc1p and its homologues in prokaryotes and higher eukaryotes. They represent paradigms of the strategies employed for the organization of sophisticated and dynamic nanostructures supporting spatio-temporal cellular organization.

Copyright © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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