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Nucleic Acids Research Advance Access originally published online on November 26, 2008
Nucleic Acids Research 2009 37(1):256-267; doi:10.1093/nar/gkn959
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Nucleic Acids Research, 2009, Vol. 37, No. 1 256-267
© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

Function and ribosomal localization of aIF6, a translational regulator shared by archaea and eukarya

Dario Benelli1,2, Stefano Marzi3, Carmine Mancone4, Tonino Alonzi4, Anna la Teana5 and Paola Londei1,*

1Dipartimento Biotecnologie Cellulari ed Ematologia, Policlinico Umberto I°, Università di Roma Sapienza, Viale Regina Elena 324, 00161 Roma, 2DIBIFIM, Università di Bari (Policlinico), Piazza Giulio Cesare, 70127 Bari, Italy, 3Institut for the Biologie Moleculaire et Cellulare CNRS, 67084 Strasbourg Cedex, France. 4National Institute for Infectious Diseases ‘L. Spallanzani’, IRCCS, Via Portuense 292, 00149 Roma and 5Istituto di Biochimica, Università Politecnica delle Marche, Via Ranieri, 60131 Ancona, Italy

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

Received October 10, 2008. Revised November 3, 2008. Accepted November 4, 2008.

The translation factor IF6 is shared by the Archaea and the Eukarya, but is not found in Bacteria. The properties of eukaryal IF6 (eIF6) have been extensively studied, but remain somewhat elusive. eIF6 behaves as a ribosome-anti-association factor and is involved in miRNA-mediated gene silencing; however, it also seems to participate in ribosome synthesis and export. Here we have determined the function and ribosomal localization of the archaeal (Sulfolobus solfataricus) IF6 homologue (aIF6). We find that aIF6 binds specifically to the 50S ribosomal subunits, hindering the formation of 70S ribosomes and strongly inhibiting translation. aIF6 is uniformly expressed along the cell cycle, but it is upregulated following both cold- and heat shock. The aIF6 ribosomal binding site lies in the middle of the 30-S interacting surface of the 50S subunit, including a number of critical RNA and protein determinants involved in subunit association. The data suggest that the IF6 protein evolved in the archaeal–eukaryal lineage to modulate translational efficiency under unfavourable environmental conditions, perhaps acquiring additional functions during eukaryotic evolution.


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