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The Giardia lamblia ribosome structure reveals divergence in several biological pathways and the mode of emetine function.

Authors :
Eiler DR
Wimberly BT
Bilodeau DY
Taliaferro JM
Reigan P
Rissland OS
Kieft JS
Source :
Structure (London, England : 1993) [Structure] 2024 Apr 04; Vol. 32 (4), pp. 400-410.e4. Date of Electronic Publication: 2024 Jan 18.
Publication Year :
2024

Abstract

Giardia lamblia is a deeply branching protist and a human pathogen. Its unusual biology presents the opportunity to explore conserved and fundamental molecular mechanisms. We determined the structure of the G. lamblia 80S ribosome bound to tRNA, mRNA, and the antibiotic emetine by cryo-electron microscopy, to an overall resolution of 2.49 Å. The structure reveals rapidly evolving protein and nucleotide regions, differences in the peptide exit tunnel, and likely altered ribosome quality control pathways. Examination of translation initiation factor binding sites suggests these interactions are conserved despite a divergent initiation mechanism. Highlighting the potential of G. lamblia to resolve conserved biological principles; our structure reveals the interactions of the translation inhibitor emetine with the ribosome and mRNA, thus providing insight into the mechanism of action for this widely used antibiotic. Our work defines key questions in G. lamblia and motivates future experiments to explore the diversity of eukaryotic gene regulation.<br />Competing Interests: Declaration of interests OSR is a member of the Molecular Cell Scientific Advisory Board and the Cell Reports Scientific Advisory Board.<br /> (Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.)

Details

Language :
English
ISSN :
1878-4186
Volume :
32
Issue :
4
Database :
MEDLINE
Journal :
Structure (London, England : 1993)
Publication Type :
Academic Journal
Accession number :
38242118
Full Text :
https://doi.org/10.1016/j.str.2023.12.015