Summary for 8RL2
Entry DOI | 10.2210/pdb8rl2/pdb |
EMDB information | 19330 |
Descriptor | 28S rRNA, 60S ribosomal protein L7a, 60S ribosomal protein L9, ... (56 entities in total) |
Functional Keywords | human, ribosome biogenesis, rix1 complex, 5s rnp, ribosome |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 52 |
Total formula weight | 2971290.32 |
Authors | Thoms, M.,Denk, T.,Beckmann, R. (deposition date: 2024-01-02, release date: 2025-01-15, Last modification date: 2025-04-30) |
Primary citation | Fiorentino, F.,Thoms, M.,Wild, K.,Denk, T.,Cheng, J.,Zeman, J.,Sinning, I.,Hurt, E.,Beckmann, R. Highly conserved ribosome biogenesis pathways between human and yeast revealed by the MDN1-NLE1 interaction and NLE1 containing pre-60S subunits. Nucleic Acids Res., 53:-, 2025 Cited by PubMed Abstract: The assembly of ribosomal subunits, primarily occurring in the nucleolar and nuclear compartments, is a highly complex process crucial for cellular function. This study reveals the conservation of ribosome biogenesis between yeast and humans, illustrated by the structural similarities of ribosomal subunit intermediates. By using X-ray crystallography and cryo-EM, the interaction between the human AAA+ ATPase MDN1 and the 60S assembly factor NLE1 is compared with the yeast homologs Rea1 and Rsa4. The MDN1-MIDAS and NLE1-Ubl complex structure at 2.3 Å resolution mirrors the highly conserved interaction patterns observed in yeast. Moreover, human pre-60S intermediates bound to the dominant negative NLE1-E85A mutant revealed at 2.8 Å resolution an architecture that largely matched the equivalent yeast structures. Conformation of rRNA, assembly factors and their interaction networks are highly conserved. Additionally, novel human pre-60S intermediates with a non-rotated 5S RNP and processed ITS2/foot structure but incomplete intersubunit surface were identified to be similar to counterparts observed in yeast. These findings confirm that the MDN1-NLE1-driven transition phase of the 60S assembly is essentially identical, supporting the idea that ribosome biogenesis is a highly conserved process across eukaryotic cells, employing an evolutionary preservation of ribosomal assembly mechanisms. PubMed: 40207627DOI: 10.1093/nar/gkaf255 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.84 Å) |
Structure validation
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