NDLI: A structural view of translation initiation in bacteria

Content Provider	Springer Nature Link
Author	Simonetti, A. Marzi, S. Jenner, L. Myasnikov, A. Romby, P. Yusupova, G. Klaholz, B. P. Yusupov, M.
Copyright Year	2008
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.
Starting Page	423
Ending Page	436
Page Count	14
File Format	PDF
ISSN	1420682X
Journal	Cellular and Molecular Life Sciences
Volume Number	66
Issue Number	3
e-ISSN	14209071
Language	English
Publisher	Birkhäuser-Verlag
Publisher Date	2008-11-17
Publisher Place	Basel
Access Restriction	Subscribed
Subject Keyword	Initiation of translation regulation of translation ribosome structure mRNA initiation factor initiator tRNA functional ribosomal complexes Cell Biology Biomedicine general Life Sciences Biochemistry
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology Molecular Medicine Pharmacology Cellular and Molecular Neuroscience

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