A structural view of translation initiation in bacteria |
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Authors: | A Simonetti S Marzi L Jenner A Myasnikov P Romby G Yusupova B P Klaholz M Yusupov |
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Institution: | (1) Department of Structural Biology and Genomics, Institute of Genetics and of Molecular and Cellular Biology, 67404 Illkirch, France;(2) INSERM, U596, 67404 Illkirch, France;(3) CNRS, UMR7104, 67404 Illkirch, France;(4) Université Louis Pasteur, 4 rue Blaise Pascal, 67070 Strasbourg, France;(5) Architecture et Réactivité de l’ARN, UPR 9002 CNRS, Institute of Molecular and Cellular Biology, 15 rue R. Descartes, 67084 Strasbourg, France |
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Abstract: | 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-tRNAfMet 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.
Received 16 July 2008; received after revision 31 August 2008; accepted 10 September 2008
A. Simonetti, S. Marzid: These authors contributed equally to this work. |
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Keywords: | " target="_blank"> Initiation of translation regulation of translation ribosome structure mRNA initiation factor initiator tRNA functional ribosomal complexes |
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