Summary for 7QV1
| Entry DOI | 10.2210/pdb7qv1/pdb |
| Related | 7QV1 7QV2 7QV3 |
| EMDB information | 14156 14157 14157 14158 14159 14160 14161 14162 14163 14164 14165 14166 |
| Descriptor | 50S ribosomal protein L32, 50S ribosomal protein L4, 50S ribosomal protein L5, ... (53 entities in total) |
| Functional Keywords | collision, muts2, disome, rqc, ssra, ribosomal collision, mrna endonuclease, ribosome |
| Biological source | Bacillus subtilis subsp. subtilis str. 168 More |
| Total number of polymer chains | 53 |
| Total formula weight | 2131509.94 |
| Authors | Filbeck, S.,Pfeffer, S. (deposition date: 2022-01-19, release date: 2022-03-09, Last modification date: 2022-03-30) |
| Primary citation | Cerullo, F.,Filbeck, S.,Patil, P.R.,Hung, H.C.,Xu, H.,Vornberger, J.,Hofer, F.W.,Schmitt, J.,Kramer, G.,Bukau, B.,Hofmann, K.,Pfeffer, S.,Joazeiro, C.A.P. Bacterial ribosome collision sensing by a MutS DNA repair ATPase paralogue. Nature, 603:509-514, 2022 Cited by PubMed Abstract: Ribosome stalling during translation is detrimental to cellular fitness, but how this is sensed and elicits recycling of ribosomal subunits and quality control of associated mRNA and incomplete nascent chains is poorly understood. Here we uncover Bacillus subtilis MutS2, a member of the conserved MutS family of ATPases that function in DNA mismatch repair, as an unexpected ribosome-binding protein with an essential function in translational quality control. Cryo-electron microscopy analysis of affinity-purified native complexes shows that MutS2 functions in sensing collisions between stalled and translating ribosomes and suggests how ribosome collisions can serve as platforms to deploy downstream processes: MutS2 has an RNA endonuclease small MutS-related (SMR) domain, as well as an ATPase/clamp domain that is properly positioned to promote ribosomal subunit dissociation, which is a requirement both for ribosome recycling and for initiation of ribosome-associated protein quality control (RQC). Accordingly, MutS2 promotes nascent chain modification with alanine-tail degrons-an early step in RQC-in an ATPase domain-dependent manner. The relevance of these observations is underscored by evidence of strong co-occurrence of MutS2 and RQC genes across bacterial phyla. Overall, the findings demonstrate a deeply conserved role for ribosome collisions in mounting a complex response to the interruption of translation within open reading frames. PubMed: 35264791DOI: 10.1038/s41586-022-04487-6 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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