Version 1
: Received: 24 September 2024 / Approved: 25 September 2024 / Online: 25 September 2024 (11:58:24 CEST)
How to cite:
Ye, J.; Trebicz-Geffen, M.; Ankri, S. Exploring the Interactome of the Queuine Salvage Protein DUF2419 in Entamoeba histolytica. Preprints2024, 2024091968. https://doi.org/10.20944/preprints202409.1968.v1
Ye, J.; Trebicz-Geffen, M.; Ankri, S. Exploring the Interactome of the Queuine Salvage Protein DUF2419 in Entamoeba histolytica. Preprints 2024, 2024091968. https://doi.org/10.20944/preprints202409.1968.v1
Ye, J.; Trebicz-Geffen, M.; Ankri, S. Exploring the Interactome of the Queuine Salvage Protein DUF2419 in Entamoeba histolytica. Preprints2024, 2024091968. https://doi.org/10.20944/preprints202409.1968.v1
APA Style
Ye, J., Trebicz-Geffen, M., & Ankri, S. (2024). Exploring the Interactome of the Queuine Salvage Protein DUF2419 in Entamoeba histolytica. Preprints. https://doi.org/10.20944/preprints202409.1968.v1
Chicago/Turabian Style
Ye, J., Meirav Trebicz-Geffen and Serge Ankri. 2024 "Exploring the Interactome of the Queuine Salvage Protein DUF2419 in Entamoeba histolytica" Preprints. https://doi.org/10.20944/preprints202409.1968.v1
Abstract
Entamoeba histolytica causes amebiasis, a significant global health issue with millions affected annually, especially in developing countries. EhDUF2419, an important protein involved in E. histolytica's queuine salvage pathway, shares homology with DNA glycosylase. However, its in-teraction network remains unclear. To explore this, we transfected E. histolytica trophozoites with a plasmid encoding Myc-tagged EhDUF2419 and achieved successful overexpression. Through immunoprecipitation with Myc antibody followed by mass spectrometry, we identified 335 proteins interacting with Myc-tagged EhDUF2419, including over 100 ribosomal proteins, along with translation initiation and elongation factors, and aminoacyl-tRNA synthetases. Ribosome purification revealed the presence of EhDUF2419 in ribosomal protein-enriched fractions. Treatment with queuosine (Q) significantly reduced EhDUF2419 protein levels and decreased Q-modified tRNA in Myc-tagged EhDUF2419 overexpressing trophozoites. This effect which is Q-dependent was not observed in strains carrying an empty vector control or overexpressing a truncated form of EhDUF2419 lacking catalytic activity. The reduction in EhDUF2419 protein levels is regulated by proteasome-mediated degradation, as evidenced by reduced degradation in the presence of MG132, a proteasome inhibitor. Our study uncovers the novel interaction of EhDUF2419 with ribosomal proteins and its regulation by the proteasome machinery, providing new insights into its role in E. histolytica and potential therapeutic strategies.
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
