|Entry||Database: EMDB / ID: EMD-21213|
|Title||Cryo-EM reconstruction of rotated 80S ribosome bound with P/E tRNA|
|Sample||Cryo-EM reconstruction of rotated 80S ribosome bound with P/E tRNA|
|Biological species||Saccharomyces cerevisiae (baker's yeast)|
|Method||single particle reconstruction / cryo EM / Resolution: 5.6 Å|
|Authors||Frank J / Sun M / Shen B / Li W|
|Funding support|| United States, 5 items |
|Citation||Journal: Proteomics / Year: 2020|
Title: A time-resolved cryo-EM Study of S. cerevisiae 80S Ribosome Protein Composition in Response to a Change in Carbon Source.
Authors: Ming Sun / Bingxin Shen / Wen Li / Parimal Samir / Christopher M Browne / Andrew J Link / Joachim Frank /
Abstract: The role of the ribosome in the regulation of gene expression has come into increased focus. It has been proposed that ribosomes are catalytic engines capable of changing their protein composition in ...The role of the ribosome in the regulation of gene expression has come into increased focus. It has been proposed that ribosomes are catalytic engines capable of changing their protein composition in response to environmental stimuli. We employed time-resolved cryo-electron microscopy (cryo-EM) techniques to identify quantitative changes in the protein composition and structure of the Saccharomyces cerevisiae 80S ribosomes after shifting the carbon source from glucose to glycerol. Using cryo-EM combined with our computational classification approach, we found that a fraction of the yeast cells' 80S ribosomes lack ribosomal proteins at the entrance and exit sites for tRNAs, including uL16(RPL10), eS1(RPS1), uS11(RPS14A/B)) and eS26(RPS26A/B). This fraction increased after a change from glucose to glycerol medium. Our quantitative structural analysis supports the hypothesis that ribosomes are dynamic complexes that alter their composition in response to changes in growth or environmental conditions. This article is protected by copyright. All rights reserved.
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_21213.map.gz / Format: CCP4 / Size: 80.2 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.66 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Additional map: Un-sharpened cryo-EM density map
-Entire Cryo-EM reconstruction of rotated 80S ribosome bound with P/E tRNA
|Entire||Name: Cryo-EM reconstruction of rotated 80S ribosome bound with P/E tRNA|
Number of components: 1
-Component #1: protein, Cryo-EM reconstruction of rotated 80S ribosome bound wit...
|Protein||Name: Cryo-EM reconstruction of rotated 80S ribosome bound with P/E tRNA|
Recombinant expression: No
|Source||Species: Saccharomyces cerevisiae (baker's yeast)|
|Specimen||Specimen state: Particle / Method: cryo EM|
|Sample solution||pH: 8|
|Vitrification||Cryogen name: ETHANE / Humidity: 100 %|
-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: 23 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: GATAN K2 SUMMIT (4k x 4k)|
|Processing||Method: single particle reconstruction / Applied symmetry: C1 (asymmetric) / Number of projections: 73418|
|3D reconstruction||Software: RELION / Resolution: 5.6 Å / Resolution method: FSC 0.143 CUT-OFF|
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