Summary for 6XU7
| Entry DOI | 10.2210/pdb6xu7/pdb |
| EMDB information | 10623 |
| Descriptor | 40S ribosomal protein SA, 40S ribosomal protein S23, 40S ribosomal protein S12, ... (83 entities in total) |
| Functional Keywords | specialised ribosome, drosophila melanogaster, testis, ribosome |
| Biological source | Drosophila melanogaster (Fruit fly) More |
| Total number of polymer chains | 83 |
| Total formula weight | 3388109.55 |
| Authors | Hopes, T.,Agapiou, M.,Norris, K.,McCarthy, C.G.P.,OConnell, M.J.,Fontana, J.,Aspden, J.L. (deposition date: 2020-01-17, release date: 2021-07-28, Last modification date: 2024-10-23) |
| Primary citation | Hopes, T.,Norris, K.,Agapiou, M.,McCarthy, C.G.P.,Lewis, P.A.,O'Connell, M.J.,Fontana, J.,Aspden, J.L. Ribosome heterogeneity in Drosophila melanogaster gonads through paralog-switching. Nucleic Acids Res., 50:2240-2257, 2022 Cited by PubMed Abstract: Ribosomes have long been thought of as homogeneous macromolecular machines, but recent evidence suggests they are heterogeneous and could be specialised to regulate translation. Here, we have characterised ribosomal protein heterogeneity across 4 tissues of Drosophila melanogaster. We find that testes and ovaries contain the most heterogeneous ribosome populations, which occurs through a combination of paralog-enrichment and paralog-switching. We have solved structures of ribosomes purified from in vivo tissues by cryo-EM, revealing differences in precise ribosomal arrangement for testis and ovary 80S ribosomes. Differences in the amino acid composition of paralog pairs and their localisation on the ribosome exterior indicate paralog-switching could alter the ribosome surface, enabling different proteins to regulate translation. One testis-specific paralog-switching pair is also found in humans, suggesting this is a conserved site of ribosome heterogeneity. Overall, this work allows us to propose that mRNA translation might be regulated in the gonads through ribosome heterogeneity, providing a potential means of ribosome specialisation. PubMed: 34283226DOI: 10.1093/nar/gkab606 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.9 Å) |
Structure validation
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