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• W1965345744 abstract "The interaction between Escherichia coli translation-initiation factor IF-1 and ribosomes was studied in binding experiments by Airfuge centrifugation. IF-1 binds to the 30S, but not to the 50S, ribosomal subunit and its binding is strongly stimulated by IF-3 and IF-2, either alone or in combination. From the dependence of the Kd of the 30S-subunit –IF-1 complex on ionic strength, it can be concluded that IF-1 binds primarily via an ionic interaction, most likely with the 16S rRNA, with the minimum number of ion pairs involved being 2.7–3.6. The 30S- subunit–IF-1 interaction is unaffected by temperature changes between 11°C and 44°C and is thus accompanied by a negligible enthalpy change. It is concluded that the interaction is an entropy-driven process triggered mainly by the release of counter ions from the RNA phosphates. Titration of 30S-subunit–IF-1 complexes with 50S subunits causes the ejection of the factor indicating that IF-1 is released from the ribosomes during the subunit association step which marks the transition from a 30S-initiation-complex to a 70S initiation complex." @default.
• W1965345744 created "2016-06-24" @default.
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• W1965345744 date "1988-12-01" @default.
• W1965345744 modified "2023-10-15" @default.
• W1965345744 title "Interaction of Escherichia coli translation-initiation factor IF-1 with ribosomes" @default.
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• W1965345744 doi "https://doi.org/10.1111/j.1432-1033.1988.tb14457.x" @default.
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