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Article Dans Une Revue Nucleic Acids Research Année : 2009

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

Dario Benelli
  • Fonction : Auteur
Carmine Mancone
  • Fonction : Auteur
Tonino Alonzi
  • Fonction : Auteur
Anna La Teana
  • Fonction : Auteur
Paola Londei
  • Fonction : Auteur

Résumé

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.

Dates et versions

hal-00477276 , version 1 (28-04-2010)

Identifiants

Citer

Dario Benelli, Stefano Marzi, Carmine Mancone, Tonino Alonzi, Anna La Teana, et al.. Function and ribosomal localization of aIF6, a translational regulator shared by archaea and eukarya.. Nucleic Acids Research, 2009, 37 (1), pp.256-67. ⟨10.1093/nar/gkn959⟩. ⟨hal-00477276⟩

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