Structural and functional domains of E coli initiation factor IF2
Identifieur interne : 001D05 ( Istex/Checkpoint ); précédent : 001D04; suivant : 001D06Structural and functional domains of E coli initiation factor IF2
Auteurs : S. Laalami [France] ; C. Sacerdot [France] ; G. Vachon [France] ; K. Mortensen [Danemark] ; H. U. Sperling-Petersen [Danemark] ; Y. Cenatiempo [France] ; M. Grunberg-Manago [France]Source :
- Biochimie [ 0300-9084 ] ; 1991.
Abstract
Initiation of translation in prokaryotes requires the participation of at least three soluble proteins: the initiation factors IF1, IF2 and IF3. Initiation factor 2, which is one of the largest proteins involved in translation (97.3 kDa) has been shown to stimulate in vitro the binding of fMet-tRNAfMet to the 30S ribosomal subunit. After formation of 70S translation intiation complex, IF2 is believed to participate in GTP hydrolysis, thereby promoting its own release. Here we review evidence which indicates the functional importance of the different structural domains of IF2, emphasizing new information obtained by in vivo experiments.
Url:
DOI: 10.1016/0300-9084(91)90191-3
Affiliations:
- Danemark, France
- Nouvelle-Aquitaine, Poitou-Charentes, Île-de-France
- Paris, Poitiers
- Université de Poitiers
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ISTEX:6EB34AF27D0525F2BA115036672D32A805678944Le document en format XML
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