Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Molecular basis of eIF5A-dependent CAT tailing in eukaryotic ribosome-associated quality control.
Journal, issue, pages	Mol Cell, Vol. 83, Issue 4, Page 607-621.e4, Year 2023
Publish date	Feb 16, 2023
Authors	Petr Tesina / Shuhei Ebine / Robert Buschauer / Matthias Thoms / Yoshitaka Matsuo / Toshifumi Inada / Roland Beckmann /
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. ...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.
External links	Mol Cell / PubMed:36804914
Methods	EM (single particle)
Resolution	2.4 - 2.9 Å
Structure data	15296 8aaf EMDB-15296, PDB-8aaf: Yeast RQC complex in state G Method: EM (single particle) / Resolution: 2.5 Å 15423 8agt EMDB-15423, PDB-8agt: Yeast RQC complex in state F Method: EM (single particle) / Resolution: 2.6 Å 15424 8agu EMDB-15424, PDB-8agu: Yeast RQC complex in state E Method: EM (single particle) / Resolution: 2.7 Å 15425 8agv EMDB-15425, PDB-8agv: Yeast RQC complex in state H Method: EM (single particle) / Resolution: 2.6 Å 15426 8agw EMDB-15426, PDB-8agw: Yeast RQC complex in state D Method: EM (single particle) / Resolution: 2.6 Å 15427 8agx EMDB-15427, PDB-8agx: Yeast RQC complex in state with the RING domain of Ltn1 in the IN position Method: EM (single particle) / Resolution: 2.4 Å 15428 8agz EMDB-15428, PDB-8agz: Yeast RQC complex in state with the RING domain of Ltn1 in the OUT position Method: EM (single particle) / Resolution: 2.6 Å EMDB-15430: Yeast RQC complex in state A (pre-initiation) Method: EM (single particle) / Resolution: 2.9 Å EMDB-15431: Yeast RQC complex in state B (A-site tRNA only) Method: EM (single particle) / Resolution: 2.8 Å EMDB-15432: Yeast RQC complex in state C Method: EM (single particle) / Resolution: 2.6 Å EMDB-15433: Yeast RQC complex in state I (translocation with A-site and E-site tRNAs) Method: EM (single particle) / Resolution: 2.8 Å EMDB-15434: Yeast RQC complex in state J Method: EM (single particle) / Resolution: 2.8 Å
Chemicals	ChemComp-MG: Unknown entry ChemComp-ZN: Unknown entry ChemComp-SPD: SPERMIDINE / Spermidine
Source	saccharomyces cerevisiae (brewer's yeast) baker's yeast (brewer's yeast)
Keywords	TRANSLATION / ribosome-associated quality control / NEMF / Listerin / CAT tailing