A time-resolved Cryo-EM study of saccharomyces cerevisiae 80S ribosome protein composition in response to a change in carbon source

Ming Sun, Bingxin Shen, Wen Li, Parimal Samir, Christopher M. Browne, Andrew J. Link, Joachim Frank

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

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.

Original languageEnglish (US)
Title of host publicationNovel Developments in Cryo-EM of Biological Molecules
Subtitle of host publicationResolution in Time and State Space
PublisherTaylor and Francis
Pages501-521
Number of pages21
ISBN (Electronic)9781000989441
ISBN (Print)9789814968768
StatePublished - Oct 6 2023
Externally publishedYes

ASJC Scopus subject areas

  • General Agricultural and Biological Sciences
  • General Biochemistry, Genetics and Molecular Biology

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