8OVE
CRYO-EM STRUCTURE OF TRYPANOSOMA BRUCEI PROCYCLIC FORM 80S RIBOSOME : TB11CS6H1 snoRNA mutant
This is a non-PDB format compatible entry.
Summary for 8OVE
| Entry DOI | 10.2210/pdb8ove/pdb |
| EMDB information | 17212 17254 17255 |
| Descriptor | SSU rRNA, 60S ribosomal protein L17, putative, 60S ribosomal protein L18a, ... (89 entities in total) |
| Functional Keywords | cryo-em, trypanosoma brucei, 80s ribosome, ribosome |
| Biological source | Trypanosoma brucei brucei More |
| Total number of polymer chains | 85 |
| Total formula weight | 3626289.78 |
| Authors | Rajan, K.S.,Yonath, A. (deposition date: 2023-04-25, release date: 2023-11-29, Last modification date: 2024-11-20) |
| Primary citation | Rajan, K.S.,Madmoni, H.,Bashan, A.,Taoka, M.,Aryal, S.,Nobe, Y.,Doniger, T.,Galili Kostin, B.,Blumberg, A.,Cohen-Chalamish, S.,Schwartz, S.,Rivalta, A.,Zimmerman, E.,Unger, R.,Isobe, T.,Yonath, A.,Michaeli, S. A single pseudouridine on rRNA regulates ribosome structure and function in the mammalian parasite Trypanosoma brucei. Nat Commun, 14:7462-7462, 2023 Cited by PubMed Abstract: Trypanosomes are protozoan parasites that cycle between insect and mammalian hosts and are the causative agent of sleeping sickness. Here, we describe the changes of pseudouridine (Ψ) modification on rRNA in the two life stages of the parasite using four different genome-wide approaches. CRISPR-Cas9 knock-outs of all four snoRNAs guiding Ψ on helix 69 (H69) of the large rRNA subunit were lethal. A single knock-out of a snoRNA guiding Ψ530 on H69 altered the composition of the 80S monosome. These changes specifically affected the translation of only a subset of proteins. This study correlates a single site Ψ modification with changes in ribosomal protein stoichiometry, supported by a high-resolution cryo-EM structure. We propose that alteration in rRNA modifications could generate ribosomes preferentially translating state-beneficial proteins. PubMed: 37985661DOI: 10.1038/s41467-023-43263-6 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.6 Å) |
Structure validation
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