Journal
FEBS LETTERS
Volume 584, Issue 18, Pages 3842-3849Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2010.08.023
Keywords
tRNA; Arc1p; Trbp111; p43; p38; p18
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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 pro-karyotes and higher eukaryotes. They represent paradigms of the strategies employed for the organization of sophisticated and dynamic nanostructures supporting spatio-temporal cellular organization. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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