A structural view of translation initiation in bacteria.
Fiche publication
Date publication
février 2009
Journal
Cellular and molecular life sciences : CMLS
Auteurs
Membres identifiés du Cancéropôle Est :
Dr KLAHOLZ Bruno, Dr ROMBY Pascale, Dr YUSUPOV Marat, Dr YUSUPOVA Gulnara, Dr SIMONETTI Angelita
Tous les auteurs :
Simonetti A, Marzi S, Jenner L, Myasnikov A, Romby P, Yusupova G, Klaholz BP, Yusupov M
Lien Pubmed
Résumé
The assembly of the protein synthesis machinery occurs during translation initiation. In bacteria, this process involves the binding of messenger RNA(mRNA) start site and fMet-tRNA(fMet) to the ribosome, which results in the formation of the first codon-anticodon interaction and sets the reading frame for the decoding of the mRNA. This interaction takes place in the peptidyl site of the 30S ribosomal subunit and is controlled by the initiation factors IF1, IF2 and IF3 to form the 30S initiation complex. The binding of the 50S subunit and the ejection of the IFs mark the irreversible transition to the elongation phase. Visualization of these ligands on the ribosome has been achieved by cryo-electron microscopy and X-ray crystallography studies, which has helped to understand the mechanism of translation initiation at the molecular level. Conformational changes associated with different functional states provide a dynamic view of the initiation process and of its regulation.
Mots clés
Bacteria, genetics, Models, Molecular, Multiprotein Complexes, metabolism, Nucleic Acid Conformation, Peptide Chain Initiation, Translational, Peptide Initiation Factors, chemistry, Protein Biosynthesis, Protein Conformation, RNA, Messenger, chemistry, RNA, Transfer, Met, chemistry, Ribosome Subunits, Small, Bacterial, chemistry
Référence
Cell. Mol. Life Sci.. 2009 Feb;66(3):423-36