A Time‐Resolved Cryo‐EM Study of Saccharomyces cerevisiae 80S Ribosome Protein Composition in Response to a Change in Carbon Source
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 employe...
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Veröffentlicht in: | Proteomics (Weinheim) 2021-01, Vol.21 (2), p.e2000125-n/a |
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description | 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. |
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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. 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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.</description><subject>Carbon sources</subject><subject>Composition</subject><subject>Computer applications</subject><subject>cryo‐electron microscopy</subject><subject>Electron microscopy</subject><subject>Entrances</subject><subject>Environmental conditions</subject><subject>Environmental effects</subject><subject>eS1 (RPS1)</subject><subject>Gene expression</subject><subject>Glucose</subject><subject>Glycerol</subject><subject>image classification</subject><subject>nutrient stress</subject><subject>Protein composition</subject><subject>Protein structure</subject><subject>Proteins</subject><subject>Ribosomal proteins</subject><subject>ribosome</subject><subject>Ribosomes</subject><subject>Saccharomyces cerevisiae</subject><subject>Structural analysis</subject><subject>Supports</subject><subject>time‐resolved methods</subject><subject>uL16 (RPL10)</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>1615-9853</issn><issn>1615-9861</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><recordid>eNqFkTtP3EAUhUdRokBIWko0Upo0u7nz9LpE1gaQQEEsqa3x-BoG2R4zYxO5S0fLb8wvyayWbJEm1X3ou0fn6hByzGDJAPjXoXN2yYEDAOPqDTlkmqlFvtLs7b5X4oB8iPEhIdkqz96TAyEAMibVIXk-pbeuw9-_Xm4w-vYJa1qE2ad5fUU341TP1Dd0Y6y9N8F3s8VILQZ8ctEZpCvY0BtX-eg7pNfBj-h6Wvhu8NGNzvc0jUl48H1EOnpqaHFv-jvc7gsTqkRs_BQsfiTvGtNG_PRaj8iPb-vb4nxx-f3soji9XFihc7aosAbk6fO6NpKpClkt0yeMS9TaZrXmmWiUso21WZWDUoA6t1ahqDTLWSWOyJed7hD844RxLDsXLbat6dFPseRSriQoCZDQz_-gD8lqn9wlKtMMJIcsUcsdZYOPMWBTDsF1Jswlg3IbUbmNqNxHlA5OXmWnqsN6j__NJAFqB_x0Lc7_kSuvry4KJoRi4g-0ip4H</recordid><startdate>202101</startdate><enddate>202101</enddate><creator>Sun, Ming</creator><creator>Shen, Bingxin</creator><creator>Li, Wen</creator><creator>Samir, Parimal</creator><creator>Browne, Christopher M.</creator><creator>Link, Andrew J.</creator><creator>Frank, Joachim</creator><general>Wiley Subscription Services, Inc</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>7QP</scope><scope>7TK</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0003-0885-5786</orcidid></search><sort><creationdate>202101</creationdate><title>A Time‐Resolved Cryo‐EM Study of Saccharomyces cerevisiae 80S Ribosome Protein Composition in Response to a Change in Carbon Source</title><author>Sun, Ming ; Shen, Bingxin ; Li, Wen ; Samir, Parimal ; Browne, Christopher M. ; Link, Andrew J. ; Frank, Joachim</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3691-bed0e2100dda415be1d4071124e66c7d6273f55cfcc7b90550e69cc5e3b6191b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Carbon sources</topic><topic>Composition</topic><topic>Computer applications</topic><topic>cryo‐electron microscopy</topic><topic>Electron microscopy</topic><topic>Entrances</topic><topic>Environmental conditions</topic><topic>Environmental effects</topic><topic>eS1 (RPS1)</topic><topic>Gene expression</topic><topic>Glucose</topic><topic>Glycerol</topic><topic>image classification</topic><topic>nutrient stress</topic><topic>Protein composition</topic><topic>Protein structure</topic><topic>Proteins</topic><topic>Ribosomal proteins</topic><topic>ribosome</topic><topic>Ribosomes</topic><topic>Saccharomyces cerevisiae</topic><topic>Structural analysis</topic><topic>Supports</topic><topic>time‐resolved methods</topic><topic>uL16 (RPL10)</topic><topic>Yeast</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sun, Ming</creatorcontrib><creatorcontrib>Shen, Bingxin</creatorcontrib><creatorcontrib>Li, Wen</creatorcontrib><creatorcontrib>Samir, Parimal</creatorcontrib><creatorcontrib>Browne, Christopher M.</creatorcontrib><creatorcontrib>Link, Andrew J.</creatorcontrib><creatorcontrib>Frank, Joachim</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Proteomics (Weinheim)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sun, Ming</au><au>Shen, Bingxin</au><au>Li, Wen</au><au>Samir, Parimal</au><au>Browne, Christopher M.</au><au>Link, Andrew J.</au><au>Frank, Joachim</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Time‐Resolved Cryo‐EM Study of Saccharomyces cerevisiae 80S Ribosome Protein Composition in Response to a Change in Carbon Source</atitle><jtitle>Proteomics (Weinheim)</jtitle><addtitle>Proteomics</addtitle><date>2021-01</date><risdate>2021</risdate><volume>21</volume><issue>2</issue><spage>e2000125</spage><epage>n/a</epage><pages>e2000125-n/a</pages><issn>1615-9853</issn><eissn>1615-9861</eissn><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. 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subjects | Carbon sources Composition Computer applications cryo‐electron microscopy Electron microscopy Entrances Environmental conditions Environmental effects eS1 (RPS1) Gene expression Glucose Glycerol image classification nutrient stress Protein composition Protein structure Proteins Ribosomal proteins ribosome Ribosomes Saccharomyces cerevisiae Structural analysis Supports time‐resolved methods uL16 (RPL10) Yeast Yeasts |
title | 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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