7OPE
RqcH DR variant bound to 50S-peptidyl-tRNA-RqcP RQC complex (rigid body refinement)
Summary for 7OPE
| Entry DOI | 10.2210/pdb7ope/pdb |
| EMDB information | 11915 13017 |
| Descriptor | 23S rRNA, 50S ribosomal protein L13, 50S ribosomal protein L14, ... (33 entities in total) |
| Functional Keywords | rqc, ribosome-associated quality control, rqcp, rqch, peptidyl-trna, large ribosomal subunit, ribosome |
| Biological source | Bacillus subtilis subsp. subtilis str. 168 More |
| Total number of polymer chains | 33 |
| Total formula weight | 1460823.89 |
| Authors | Crowe-McAuliffe, C.,Wilson, D.N. (deposition date: 2021-05-31, release date: 2021-07-21, Last modification date: 2024-11-06) |
| Primary citation | Takada, H.,Crowe-McAuliffe, C.,Polte, C.,Sidorova, Z.Y.,Murina, V.,Atkinson, G.C.,Konevega, A.L.,Ignatova, Z.,Wilson, D.N.,Hauryliuk, V. RqcH and RqcP catalyze processive poly-alanine synthesis in a reconstituted ribosome-associated quality control system. Nucleic Acids Res., 49:8355-8369, 2021 Cited by PubMed Abstract: In the cell, stalled ribosomes are rescued through ribosome-associated protein quality-control (RQC) pathways. After splitting of the stalled ribosome, a C-terminal polyalanine 'tail' is added to the unfinished polypeptide attached to the tRNA on the 50S ribosomal subunit. In Bacillus subtilis, polyalanine tailing is catalyzed by the NEMF family protein RqcH, in cooperation with RqcP. However, the mechanistic details of this process remain unclear. Here we demonstrate that RqcH is responsible for tRNAAla selection during RQC elongation, whereas RqcP lacks any tRNA specificity. The ribosomal protein uL11 is crucial for RqcH, but not RqcP, recruitment to the 50S subunit, and B. subtilis lacking uL11 are RQC-deficient. Through mutational mapping, we identify critical residues within RqcH and RqcP that are important for interaction with the P-site tRNA and/or the 50S subunit. Additionally, we have reconstituted polyalanine-tailing in vitro and can demonstrate that RqcH and RqcP are necessary and sufficient for processivity in a minimal system. Moreover, the in vitro reconstituted system recapitulates our in vivo findings by reproducing the importance of conserved residues of RqcH and RqcP for functionality. Collectively, our findings provide mechanistic insight into the role of RqcH and RqcP in the bacterial RQC pathway. PubMed: 34255840DOI: 10.1093/nar/gkab589 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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