Publications
2009
Benelli D, Marzi S, Mancone C, Alonzi T, la Teana A, Londei P
Function and ribosomal localization of aIF6, a translational regulator shared by archaea and eukarya Article de journal
Dans: Nucleic Acids Res, vol. 37, no. 1, p. 256-267, 2009, ISBN: 19036786, (1362-4962 (Electronic) Journal Article Research Support, Non-U.S. Gov't).
Résumé | Liens | BibTeX | Étiquettes: 23S/chemistry/metabolism Ribosomal Proteins/metabolism Ribosome Subunits, Archaeal Proteins/analysis/chemistry/*metabolism Base Sequence Binding Sites Cell Cycle Cloning, Archaeal/*metabolism Ribosomes/metabolism Sulfolobus solfataricus/*genetics/metabolism, Large, Molecular Eukaryotic Initiation Factors/chemistry Models, Molecular Molecular Sequence Data Prokaryotic Initiation Factors/analysis/chemistry/*metabolism *Protein Biosynthesis RNA, Ribosomal, ROMBY, Unité ARN
@article{,
title = {Function and ribosomal localization of aIF6, a translational regulator shared by archaea and eukarya},
author = {D Benelli and S Marzi and C Mancone and T Alonzi and A la Teana and P Londei},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=19036786},
isbn = {19036786},
year = {2009},
date = {2009-01-01},
journal = {Nucleic Acids Res},
volume = {37},
number = {1},
pages = {256-267},
abstract = {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.},
note = {1362-4962 (Electronic)
Journal Article
Research Support, Non-U.S. Gov't},
keywords = {23S/chemistry/metabolism Ribosomal Proteins/metabolism Ribosome Subunits, Archaeal Proteins/analysis/chemistry/*metabolism Base Sequence Binding Sites Cell Cycle Cloning, Archaeal/*metabolism Ribosomes/metabolism Sulfolobus solfataricus/*genetics/metabolism, Large, Molecular Eukaryotic Initiation Factors/chemistry Models, Molecular Molecular Sequence Data Prokaryotic Initiation Factors/analysis/chemistry/*metabolism *Protein Biosynthesis RNA, Ribosomal, ROMBY, Unité ARN},
pubstate = {published},
tppubtype = {article}
}