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Assembling the archaeal ribosome: roles for translation-factor-related GTPases

Blombach, F; Brouns, SJJ; van der Oost, J; (2011) Assembling the archaeal ribosome: roles for translation-factor-related GTPases. BIOCHEM SOC T , 39 45 - 50. 10.1042/BST0390045.

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Abstract

The assembly of ribosomal subunits from their individual components (rRNA and ribosomal proteins) requires the assistance of a multitude of factors in order to control and increase the efficiency of the assembly process. GTPases of the TRAFAC (translation-factor-related) class constitute a major type of ribosome-assembly factor in Eukaryota and Bacteria. They are thought to aid the stepwise assembly of ribosomal subunits through a 'molecular switch' mechanism that involves conformational changes in response to GTP hydrolysis. Most conserved TRAFAC GTPases are involved in ribosome assembly or other translation-associated processes. They typically interact with ribosomal subunits, but in many cases, the exact role that these GTPases play remains unclear. Previous studies almost exclusively focused on the systems of Bacteria and Eukaryota. Archaea possess several conserved TRAFAC GTPases as well, with some GTPase families being present only in the archaeo-eukaryotic lineage. In the present paper, we review the occurrence of TRAFAC GTPases with translation-associated functions in Archaea.

Type: Article
Title: Assembling the archaeal ribosome: roles for translation-factor-related GTPases
DOI: 10.1042/BST0390045
Keywords: archaeon, GTPase, ribosome assembly, translation-factor-related GTPase (TRAFAC GTPase), GTP-BINDING PROTEIN, CIRCULARLY PERMUTED GTPASE, BACILLUS-SUBTILIS, CRYSTAL-STRUCTURE, ELONGATION-FACTOR, SUBUNIT, EVOLUTION, DOMAIN, OBG, REVEALS
UCL classification: UCL > School of Life and Medical Sciences
UCL > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > School of Life and Medical Sciences > Faculty of Life Sciences > Biosciences (Division of) > Structural and Molecular Biology
URI: http://discovery.ucl.ac.uk/id/eprint/1326364
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