6SV4
The cryo-EM structure of SDD1-stalled collided trisome.
This is a non-PDB format compatible entry.
Summary for 6SV4
| Entry DOI | 10.2210/pdb6sv4/pdb |
| EMDB information | 10315 |
| Descriptor | 25S rRNA, 60S ribosomal protein L8-A, 60S ribosomal protein L9-A, ... (82 entities in total) |
| Functional Keywords | trisome, ribosome, collision, stalling, translation |
| Biological source | Saccharomyces cerevisiae More |
| Total number of polymer chains | 242 |
| Total formula weight | 9522691.32 |
| Authors | Tesina, P.,Buschauer, R.,Cheng, J.,Becker, T.,Beckmann, R. (deposition date: 2019-09-17, release date: 2020-03-04, Last modification date: 2024-10-16) |
| Primary citation | Matsuo, Y.,Tesina, P.,Nakajima, S.,Mizuno, M.,Endo, A.,Buschauer, R.,Cheng, J.,Shounai, O.,Ikeuchi, K.,Saeki, Y.,Becker, T.,Beckmann, R.,Inada, T. RQT complex dissociates ribosomes collided on endogenous RQC substrate SDD1. Nat.Struct.Mol.Biol., 27:323-332, 2020 Cited by PubMed Abstract: Ribosome-associated quality control (RQC) represents a rescue pathway in eukaryotic cells that is triggered upon translational stalling. Collided ribosomes are recognized for subsequent dissociation followed by degradation of nascent peptides. However, endogenous RQC-inducing sequences and the mechanism underlying the ubiquitin-dependent ribosome dissociation remain poorly understood. Here, we identified SDD1 messenger RNA from Saccharomyces cerevisiae as an endogenous RQC substrate and reveal the mechanism of its mRNA-dependent and nascent peptide-dependent translational stalling. In vitro translation of SDD1 mRNA enabled the reconstitution of Hel2-dependent polyubiquitination of collided disomes and, preferentially, trisomes. The distinct trisome architecture, visualized using cryo-EM, provides the structural basis for the more-efficient recognition by Hel2 compared with that of disomes. Subsequently, the Slh1 helicase subunit of the RQC trigger (RQT) complex preferentially dissociates the first stalled polyubiquitinated ribosome in an ATP-dependent manner. Together, these findings provide fundamental mechanistic insights into RQC and its physiological role in maintaining cellular protein homeostasis. PubMed: 32203490DOI: 10.1038/s41594-020-0393-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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