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The complete, functional and dynamic cycle of the bacterial Initiation Factor 3

Jose A. Nakamoto, Roberto Spurio, Andrey L. Konevega, Attilio Fabbretti, View ORCID ProfilePohl Milón
doi: https://doi.org/10.1101/579326
Jose A. Nakamoto
1Laboratory of Applied Biophysics and Biochemistry, Centre for Research and Innovation, Health Sciences Faculty, Universidad Peruana de Ciencias Aplicadas (UPC), 15023 Lima, Peru
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Roberto Spurio
2Laboratory of Genetics, School of Biosciences and Veterinary Medicine, University of Camerino, 62032 Camerino, Italy
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Andrey L. Konevega
3Petersburg Nuclear Physics Institute, NRC “Kurchatov Institute”, 188300 Gatchina, Russia
4NRC “Kurchatov Institute”, Moscow 123182, Russia
5Peter the Great St. Petersburg Polytechnic University, Saint Petersburg 195251, Russia
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Attilio Fabbretti
2Laboratory of Genetics, School of Biosciences and Veterinary Medicine, University of Camerino, 62032 Camerino, Italy
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Pohl Milón
1Laboratory of Applied Biophysics and Biochemistry, Centre for Research and Innovation, Health Sciences Faculty, Universidad Peruana de Ciencias Aplicadas (UPC), 15023 Lima, Peru
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  • ORCID record for Pohl Milón
  • For correspondence: pmilon@upc.edu.pe
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Abstract

Initiation factor 3 (IF3) is an essential protein that enhances the fidelity and speed of bacterial initiation of mRNA translation. The dynamic interplay between the two independent IF3 domains, their alternative binding sites, and the mechanism that ensures translation initiation fidelity remains elusive. Here, we show that the functional positioning of IF3 domains occurs at velocities ranging over two orders of magnitude, driven by each 30S initiation ligand. IF1 and IF2 rapidly promote the accommodation of IF3 on the 30S platform with the C-terminal domain moving towards the P site. Reversion of this movement is triggered by decoding the mRNA start codon and rate limits translation initiation. Binding of the tRNA results in the concomitant accommodation of the N-terminal domain of IF3, largely dependent on the mRNA and initiator tRNA. 70S initiation complex formation promotes the closing and dissociation of IF3, recycling the factor for a new round of translation initiation. Altogether our results unveil the kinetic spectrum of IF3 conformations and highlight fundamental movements of the factor that ensure accurate translation initiation.

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Posted March 16, 2019.
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The complete, functional and dynamic cycle of the bacterial Initiation Factor 3
Jose A. Nakamoto, Roberto Spurio, Andrey L. Konevega, Attilio Fabbretti, Pohl Milón
bioRxiv 579326; doi: https://doi.org/10.1101/579326
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The complete, functional and dynamic cycle of the bacterial Initiation Factor 3
Jose A. Nakamoto, Roberto Spurio, Andrey L. Konevega, Attilio Fabbretti, Pohl Milón
bioRxiv 579326; doi: https://doi.org/10.1101/579326

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