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• W2080294804 startingPage "69" @default.
• W2080294804 abstract "Bovine mitochondrial translational initiation factor 2 (IF-2(mt)) is organized into four domains, an N-terminal domain, a central G-domain and two C-terminal domains. These domains correspond to domains III-VI in the six-domain model of Escherichia coli IF-2. Variants in IF-2(mt) were prepared and tested for their abilities to bind the small (28S) subunit of the mitochondrial ribosome. The binding of wild-type IF-2(mt) was strong (K(d) approximately 10-20 nM) and was not affected by fMet-tRNA. Deletion of the N-terminal domain substantially reduced the binding of IF-2(mt) to 28S subunits. However, the addition of fMet-tRNA stimulated the binding of this variant at least 2-fold demonstrating that contacts between fMet-tRNA and IF-2(mt) can stabilize the binding of this factor to 28S subunits. No binding was observed for IF-2(mt) variants lacking the G-domain which probably plays a critical role in organizing the structure of IF-2(mt). IF-2(mt) contains a 37-amino acid insertion region between domains V and VI that is not found in the prokaryotic factors. Mutations in this region caused a significant reduction in the ability of the factor to promote initiation complex formation and to bind 28S subunits." @default.
• W2080294804 created "2016-06-24" @default.
• W2080294804 creator A5005759667 @default.
• W2080294804 creator A5056487298 @default.
• W2080294804 date "2005-06-01" @default.
• W2080294804 modified "2023-09-26" @default.
• W2080294804 title "The interaction of mitochondrial translational initiation factor 2 with the small ribosomal subunit" @default.
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• W2080294804 doi "https://doi.org/10.1016/j.bbapap.2005.03.009" @default.
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