FEBS Letters
Volume 584, Issue 18 , Pages 3842-3849, 24 September 2010

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

Edited by Michael Ibba

  • Eleftherios Karanasios

      Affiliations

    • Laboratory of Biochemistry, School of Medicine, University of Thessaly, BIOPOLIS, Larissa 41110, Greece
    • Present address: Cambridge Institute for Medical Research, Wellcome Trust/MRC Building, Addenbrooke’s Hospital, Hills Road, Cambridge CB2 0XY, UK.
    • ,
  • George Simos

      Affiliations

    • Laboratory of Biochemistry, School of Medicine, University of Thessaly, BIOPOLIS, Larissa 41110, Greece
    • Institute of Biomedical Research and Technology (BIOMED), 51 Papanastasiou Str., Larissa 41222, Greece
    • Corresponding Author InformationCorresponding author at: Laboratory of Biochemistry, School of Medicine, University of Thessaly, BIOPOLIS, Larissa 41110, Greece. Fax: +30 2410 685545.

Received 23 July 2010; received in revised form 14 August 2010; accepted 16 August 2010. published online 20 August 2010.

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.

Keywords: tRNA, Arc1p, Trbp111, p43, p38, p18

Abbreviations: aaRS, aminoacyl-tRNA synthetase, NLS, nuclear localization signal, NES, nuclear export signal

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PII: S0014-5793(10)00679-4

doi:10.1016/j.febslet.2010.08.023

FEBS Letters
Volume 584, Issue 18 , Pages 3842-3849, 24 September 2010

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