Summary for 8AGV
Entry DOI | 10.2210/pdb8agv/pdb |
EMDB information | 15425 |
Descriptor | 60S ribosomal protein L15-A, 60S ribosomal protein L24-A, 60S ribosomal protein L25, ... (55 entities in total) |
Functional Keywords | ribosome-associated quality control, nemf, listerin, cat tailing, translation |
Biological source | Saccharomyces cerevisiae (baker's yeast) More |
Total number of polymer chains | 54 |
Total formula weight | 2401125.22 |
Authors | Tesina, P.,Buschauer, R.,Beckmann, R. (deposition date: 2022-07-20, release date: 2023-03-08, Last modification date: 2024-10-23) |
Primary citation | Tesina, P.,Ebine, S.,Buschauer, R.,Thoms, M.,Matsuo, Y.,Inada, T.,Beckmann, R. Molecular basis of eIF5A-dependent CAT tailing in eukaryotic ribosome-associated quality control. Mol.Cell, 83:607-621.e4, 2023 Cited by PubMed Abstract: Ribosome-associated quality control (RQC) is a conserved process degrading potentially toxic truncated nascent peptides whose malfunction underlies neurodegeneration and proteostasis decline in aging. During RQC, dissociation of stalled ribosomes is followed by elongation of the nascent peptide with alanine and threonine residues, driven by Rqc2 independently of mRNA, the small ribosomal subunit and guanosine triphosphate (GTP)-hydrolyzing factors. The resulting CAT tails (carboxy-terminal tails) and ubiquitination by Ltn1 mark nascent peptides for proteasomal degradation. Here we present ten cryogenic electron microscopy (cryo-EM) structures, revealing the mechanistic basis of individual steps of the CAT tailing cycle covering initiation, decoding, peptidyl transfer, and tRNA translocation. We discovered eIF5A as a crucial eukaryotic RQC factor enabling peptidyl transfer. Moreover, we observed dynamic behavior of RQC factors and tRNAs allowing for processivity of the CAT tailing cycle without additional energy input. Together, these results elucidate key differences as well as common principles between CAT tailing and canonical translation. PubMed: 36804914DOI: 10.1016/j.molcel.2023.01.020 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.6 Å) |
Structure validation
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