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A Time‐Resolved Cryo‐EM Study of Saccharomyces cerevisiae 80S Ribosome Protein Composition in Response to a Change in Carbon Source
Author(s) -
Sun Ming,
Shen Bingxin,
Li Wen,
Samir Parimal,
Browne Christopher M.,
Link Andrew J.,
Frank Joachim
Publication year - 2021
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.202000125
Subject(s) - ribosome , saccharomyces cerevisiae , biology , eukaryotic ribosome , ribosomal protein , biochemistry , glycerol , yeast , composition (language) , ribosomal rna , cryo electron microscopy , microbiology and biotechnology , biophysics , gene , rna , linguistics , philosophy
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.