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

Eiler, Daniel R.; Wimberly, Brian T.; Bilodeau, Danielle Y.; Taliaferro, J. Matthew; Reigan, Philip; Rissland, Olivia S.; Kieft, Jeffrey S.

doi:10.1016/j.str.2023.12.015

Cited by 4 publications

(2 citation statements)

References 71 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, for both anisomycin and narciclasine, translation rates for socRNAs translated by two ribosomes was substantially higher than expected, indicative of ribosome cooperativity (Figure 3K and 3L). Interestingly, both anisomycin and narciclasine likely inhibit the step of peptide bond formation in the translation elongation cycle (Garreau de Loubresse et al, 2014), similar to the Xbp1 sequence (Shanmuganathan et al ., 2019) and the polylysine peptide encoded by the poly(A) sequence (Chandrasekaran et al ., 2019) (although poly(A) sequences also inhibit the decoding step (Tesina et al, 2020)), while emetine inhibits the mRNA-tRNA translocation step (Eiler et al, 2024; Wong et al, 2014), suggesting that ribosome cooperativity may promote peptide bond formation. Additional steps in the elongation cycle may also be facilitated by ribosome cooperativity, as RNA structures, which are also targeted by ribosome cooperativity, likely inhibit the translocation step of the elongation cycle (Caliskan et al, 2014; Namy et al ., 2006)(See Discussion).…”

Section: Resultsmentioning

confidence: 99%

Ribosome cooperativity promotes fast and efficient translation

Madern,

Yang,

Tanenbaum

2024

Preprint

View full text Add to dashboard Cite

The genetic information stored in mRNA is decoded by ribosomes during mRNA translation. mRNAs are typically translated by multiple ribosomes simultaneously, but it is unclear if different ribosomes translating the same mRNA functionally interact with each other. Here, we combine single-ribosome imaging and simulations to compare translation dynamics of individual ribosomes in either monosomes or polysomes to determine how ribosomes interact during translation. We find that ribosomes frequently undergo transient collisions, but that transient collisions, unlike persistent collisions, escape detection by cellular quality control pathways. Instead, our results indicate that transient ribosome collisions promote productive translation by suppressing ribosome pausing when ribosomes encounter problems, a process we term ribosome cooperativity. Ribosome cooperativity also suppresses ribosome recycling on problematic sequences, likely by reducing pause duration, thus stimulating processive translation. Together, our results show that ribosomes cooperate during translation to ensure fast and efficient translation.

show abstract

Section: Resultsmentioning

confidence: 99%

Ribosome cooperativity promotes fast and efficient translation

Madern,

Yang,

Tanenbaum

2024

Preprint

View full text Add to dashboard Cite

show abstract

“…The high-resolution ribosome structures from other protozoans: Trypanosoma brucei 19 , Plasmodium falciparum 20 , Leishmania donovani 21 , Trichomonas vaginalis and Toxoplasma gondii 22 , Euglena gracilis 23 Giardia lamblia 24,25,26 have revealed the speciesspecific unique features of their architecture and protein synthesis. The atomic details for E. histolytica ribosome architecture are absent as no structure is available.…”

Section: Introductionmentioning

confidence: 99%

Cryo- EM structure of ribosome from pathogenic protozoa Entamoeba histolytica, reveals unique features of its architecture

Kaushal,

Sharma,

Mishra

et al. 2024

Preprint

View full text Add to dashboard Cite

Entamoeba histolytica, an anaerobic parasite protozoan, is the causative agent of amoebiasis, the bloody diarrhea, and liver abscesses in humans. Amoebiasis is more predominant in tropical areas with poor sanitation conditions, and it remains the fourth leading cause of death due to a protozoan infection. E. histolytica life cycle spans between an infective ‘cyst stage’ and an active disease-causing ‘trophozoite stage’. We have isolated ribosomes from the trophozoite stage and determined its single particle cryo- EM structures. The 53S, ribosome large subunit (LSU), at 2.8 Å resolution, and the 75S, associated ribosome, at 3.3 Å resolution. The E. histolytica possesses a reduced ribosome with a conserved core, and the periphery evolved with Entamoeba specific unique features. The most notable features are the presence of the rRNA triple helix near the peptide exit tunnel on LSU and the co-evolution of rRNA expansion segments and extensions in r-proteins. These structures provide valuable insights into the evolutionary adaption of the Entamoeba translational machinery and could be explored further for amoebicidal therapeutic intervention.

show abstract

A glimpse into Giardia lamblia unique translational machinery

Querido

2024

Structure

View full text Add to dashboard Cite

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

Cited by 4 publications

References 71 publications

Ribosome cooperativity promotes fast and efficient translation

Ribosome cooperativity promotes fast and efficient translation

Cryo- EM structure of ribosome from pathogenic protozoa Entamoeba histolytica, reveals unique features of its architecture

A glimpse into Giardia lamblia unique translational machinery

Contact Info

Product

Resources

About