PMID:1805969
| Citation |
Laalami, S, Sacerdot, C, Vachon, G, Mortensen, K, Sperling-Petersen, HU, Cenatiempo, Y and Grunberg-Manago, M (1991) Structural and functional domains of E coli initiation factor IF2. Biochimie 73:1557-66 |
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| 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-tRNA(fMet) to the 30S ribosomal subunit. After formation of 70S translation initiation 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. |
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| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Blotting, Western; Escherichia coli/genetics; GTP-Binding Proteins/metabolism; Molecular Sequence Data; Mutation; Peptide Initiation Factors/chemistry; Peptide Initiation Factors/genetics; Peptide Initiation Factors/metabolism; Plasmids; Prokaryotic Initiation Factor-2; Protein Biosynthesis; Protein Conformation |
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