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-Structure paper
タイトル | A Time-Resolved Cryo-EM Study of Saccharomyces cerevisiae 80S Ribosome Protein Composition in Response to a Change in Carbon Source. |
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ジャーナル・号・ページ | Proteomics, Vol. 21, Issue 2, Page e2000125, Year 2021 |
掲載日 | 2020年12月2日 |
著者 | Ming Sun / Bingxin Shen / Wen Li / Parimal Samir / Christopher M Browne / Andrew J Link / Joachim Frank / |
PubMed 要旨 | The role of the ribosome in the regulation of gene expression has come into increased focus. It is 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 is proposed that ribosomes are catalytic engines capable of changing their protein composition in response to environmental stimuli. Time-resolved cryo-electron microscopy (cryo-EM) techniques are employed 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 the computational classification approach, it is 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. The quantitative structural analysis supports the hypothesis that ribosomes are dynamic complexes that alter their composition in response to changes in growth or environmental conditions. |
リンク | Proteomics / PubMed:33007145 |
手法 | EM (単粒子) |
解像度 | 5.6 - 9.8 Å |
構造データ | EMDB-21213: EMDB-21214: EMDB-21215: EMDB-21216: EMDB-21217: EMDB-21218: |
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