|Entry||Database: EMDB / ID: EMD-4799|
|Title||B.subtilis 50S subunit-nascent chain-tRNA complex|
|Sample||Bacillus subtilis 50S subunit-nascent chain-tRNA complex|
|Biological species||Bacillus subtilis subsp. subtilis str. 168 (bacteria)|
|Method||single particle reconstruction / cryo EM / Resolution: 3.8 Å|
|Authors||Lytvynenko I / Paternoga H / Thrun A / Balke A / Mueller T / Nagler K / Chiang CH / Tsaprailis G / Anders S / Maupin-Furlow JA / Bischofs I / Spahn CMT / Joazeiro CAP|
|Citation||Journal: Cell / Year: 2019|
Title: Alanine Tails Signal Proteolysis in Bacterial Ribosome-Associated Quality Control.
Authors: Iryna Lytvynenko / Helge Paternoga / Anna Thrun / Annika Balke / Tina A Müller / Christina H Chiang / Katja Nagler / George Tsaprailis / Simon Anders / Ilka Bischofs / Julie A Maupin-Furlow / Christian M T Spahn / Claudio A P Joazeiro /
Abstract: In ribosome-associated quality control (RQC), Rqc2/NEMF closely supports the E3 ligase Ltn1/listerin in promoting ubiquitylation and degradation of aberrant nascent-chains obstructing large (60S) ...In ribosome-associated quality control (RQC), Rqc2/NEMF closely supports the E3 ligase Ltn1/listerin in promoting ubiquitylation and degradation of aberrant nascent-chains obstructing large (60S) ribosomal subunits-products of ribosome stalling during translation. However, while Ltn1 is eukaryote-specific, Rqc2 homologs are also found in bacteria and archaea; whether prokaryotic Rqc2 has an RQC-related function has remained unknown. Here, we show that, as in eukaryotes, a bacterial Rqc2 homolog (RqcH) recognizes obstructed 50S subunits and promotes nascent-chain proteolysis. Unexpectedly, RqcH marks nascent-chains for degradation in a direct manner, by appending C-terminal poly-alanine tails that act as degrons recognized by the ClpXP protease. Furthermore, RqcH acts redundantly with tmRNA/ssrA and protects cells against translational and environmental stresses. Our results uncover a proteolytic-tagging mechanism with implications toward the function of related modifications in eukaryotes and suggest that RQC was already active in the last universal common ancestor (LUCA) to help cope with incomplete translation.
|Date||Deposition: Apr 10, 2019 / Header (metadata) release: Jun 12, 2019 / Map release: Jun 12, 2019 / Update: Jun 12, 2019|
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_4799.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.25 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire Bacillus subtilis 50S subunit-nascent chain-tRNA complex
|Entire||Name: Bacillus subtilis 50S subunit-nascent chain-tRNA complex|
Number of components: 1
-Component #1: protein, Bacillus subtilis 50S subunit-nascent chain-tRNA complex
|Protein||Name: Bacillus subtilis 50S subunit-nascent chain-tRNA complex|
Recombinant expression: No
|Mass||Theoretical: 25 kDa|
|Source||Species: Bacillus subtilis subsp. subtilis str. 168 (bacteria)|
|Source (engineered)||Expression System: Bacillus subtilis subsp. subtilis str. 168 (bacteria)|
|Specimen||Specimen state: Particle / Method: cryo EM|
|Sample solution||pH: 7.5|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Tecnai Polara / Image courtesy: FEI Company
|Imaging||Microscope: FEI POLARA 300|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 30 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: GATAN K2 SUMMIT (4k x 4k)|
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