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Nucleic Acids Research 2005 33(6):1804-1812; doi:10.1093/nar/gki321
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Published online 23 March 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

The archaeal eIF2 homologue: functional properties of an ancient translation initiation factor

Nadia Pedullà1, Rocco Palermo1, David Hasenöhrl2, Udo Bläsi2, Piero Cammarano1 and Paola Londei1,3,*

1Department of Cellular Biotechnology and Hematology, University of Rome La Sapienza Viale Regina Elena 324, 00161 Rome, Italy 2Max F. Perutz Laboratories, Department of Microbiology and Immunobiology, University Departments at the Vienna Biocenter Dr Bohrgasse 9, 1030 Vienna, Austria 3Department of Medical Biochemistry, Biology and Physics (DIBIFIM), University of Bari Piazza Giulio Cesare, 70124 Bari, Italy

*To whom correspondence should be addressed. Tel: +39 06 4940463; Fax: +39 06 4462891; Email: londei{at}bce.uniroma1.it

Received February 4, 2005. Revised March 4, 2005. Accepted March 4, 2005.

The eukaryotic translation initiation factor 2 (eIF2) is pivotal for delivery of the initiator tRNA (tRNAi) to the ribosome. Here, we report the functional characterization of the archaeal homologue, a/eIF2. We have cloned the genes encoding the three subunits of a/eIF2 from the thermophilic archaeon Sulfolobus solfataricus, and have assayed the activities of the purified recombinant proteins in vitro. We demonstrate that the trimeric factor reconstituted from the recombinant polypeptides has properties similar to those of its eukaryal homologue: it interacts with GTP and Met-tRNAi, and stimulates binding of the latter to the small ribosomal subunit. However, the archaeal protein differs in some functional aspects from its eukaryal counterpart. In contrast to eIF2, a/eIF2 has similar affinities for GDP and GTP, and the ß-subunit does not contribute to tRNAi binding. The detailed analysis of the complete trimer and of its isolated subunits is discussed in light of the evolutionary history of the eIF2-like proteins.


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