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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. ek340@cam.ac.uk

Abstract

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.

PMID:
20728442
[PubMed - indexed for MEDLINE]
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