A conformational switch in initiation factor 2 controls the fidelity of translation initiation in bacteria

Kelvin Caban, Michael Pavlov, Måns Ehrenberg and Ruben L. Gonzalez ()
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Kelvin Caban: Columbia University
Michael Pavlov: BMC, Uppsala University
Måns Ehrenberg: BMC, Uppsala University
Ruben L. Gonzalez: Columbia University

Nature Communications, 2017, vol. 8, issue 1, 1-11

Abstract: Abstract Initiation factor (IF) 2 controls the fidelity of translation initiation by selectively increasing the rate of 50S ribosomal subunit joining to 30S initiation complexes (ICs) that carry an N-formyl-methionyl-tRNA (fMet-tRNAfMet). Previous studies suggest that rapid 50S subunit joining involves a GTP- and fMet-tRNAfMet-dependent “activation” of IF2, but a lack of data on the structure and conformational dynamics of 30S IC-bound IF2 has precluded a mechanistic understanding of this process. Here, using an IF2-tRNA single-molecule fluorescence resonance energy transfer signal, we directly observe the conformational switch that is associated with IF2 activation within 30S ICs that lack IF3. Based on these results, we propose a model of IF2 activation that reveals how GTP, fMet-tRNAfMet, and specific structural elements of IF2 drive and regulate this conformational switch. Notably, we find that domain III of IF2 plays a pivotal, allosteric, role in IF2 activation, suggesting that this domain can be targeted for the development of novel antibiotics.

Date: 2017
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DOI: 10.1038/s41467-017-01492-6

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