EMD-29495
40S subunit of the Giardia lamblia 80S ribosome
EMD-29495
Single-particle2.94 Å
Deposition: 20/01/2023
Map released: 24/01/2024
Last modified: 17/04/2024
Sample Organism:
Giardia intestinalis assemblage A
Sample: 60S ribosomal subunit of the 80S Giardia intestinalis assemblage A ribosome
Fitted models: 8fvy (Avg. Q-score: 0.51)
Deposition Authors: Eiler DR , Wimberly BT , Bilodeau DY , Rissland OS , Kieft JS
Sample: 60S ribosomal subunit of the 80S Giardia intestinalis assemblage A ribosome
Fitted models: 8fvy (Avg. Q-score: 0.51)
Deposition Authors: Eiler DR , Wimberly BT , Bilodeau DY , Rissland OS , Kieft JS
The Giardia lamblia ribosome structure reveals divergence in several biological pathways and the mode of emetine function.
Eiler DR ,
Wimberly BT ,
Bilodeau DY ,
Taliaferro JM,
Reigan P ,
Rissland OS ,
Kieft JS
(2024) Structure , 32 , 400
(2024) Structure , 32 , 400
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.
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.