Hyper-swivel head domain motions are required for complete mRNA-TRNA translocation and ribosome resetting

Wataru Nishima, Dylan Girodat, Mikael Holm, Emily J. Rundlet, Jose L. Alejo, Kara Fischer, Scott C. Blanchard, Karissa Y. Sanbonmatsu

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

Translocation of messenger RNA (mRNA) and transfer RNA (tRNA) substrates through the ribosome during protein synthesis, an exemplar of directional molecular movement in biology, entails a complex interplay of conformational, compositional, and chemical changes. The molecular determinants of early translocation steps have been investigated rigorously. However, the elements enabling the ribosome to complete translocation and reset for subsequent protein synthesis reactions remain poorly understood. Here, we have combined molecular simulations with single-molecule fluorescence resonance energy transfer imaging to gain insights into the rate-limiting events of the translocation mechanism. We find that diffusive motions of the ribosomal small subunit head domain to hyper-swivelled positions, governed by universally conserved rRNA, can maneuver the mRNA and tRNAs to their fully translocated positions. Subsequent engagement of peptidyl-TRNA and disengagement of deacyl-TRNA from mRNA, within their respective small subunit binding sites, facilitate the ribosome resetting mechanism after translocation has occurred to enable protein synthesis to resume.

Original languageEnglish (US)
Pages (from-to)8302-8320
Number of pages19
JournalNucleic acids research
Volume50
Issue number14
DOIs
StatePublished - Aug 12 2022

Bibliographical note

Publisher Copyright:
© 2022 Published by Oxford University Press on behalf of Nucleic Acids Research.

PubMed: MeSH publication types

  • Journal Article
  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

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