Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2048424 | FEBS Letters | 2010 | 8 Pages |
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.
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Authors
Eleftherios Karanasios, George Simos,