Importance of diphthamide modified EF2 for translational accuracy and competitive cell growth in yeast.
Identifieur interne : 000577 ( Main/Exploration ); précédent : 000576; suivant : 000578Importance of diphthamide modified EF2 for translational accuracy and competitive cell growth in yeast.
Auteurs : Harmen Hawer [Allemagne] ; Koray Ütkür [Allemagne] ; Meike Arend [Allemagne] ; Klaus Mayer [Allemagne] ; Lorenz Adrian [Allemagne] ; Ulrich Brinkmann [Allemagne] ; Raffael Schaffrath [Allemagne]Source :
- PloS one [ 1932-6203 ] ; 2018.
Descripteurs français
- KwdFr :
- Anisomycine (pharmacologie), Biosynthèse des protéines (effets des médicaments et des substances chimiques), Caféine (pharmacologie), Cinnamates (pharmacologie), Division cellulaire (effets des médicaments et des substances chimiques), Délétion de gène (MeSH), Facteur-1 d'élongation de la chaîne peptidique (génétique), Facteur-1 d'élongation de la chaîne peptidique (métabolisme), Facteur-2 d'élongation de la chaîne peptidique (déficit), Facteur-2 d'élongation de la chaîne peptidique (génétique), Histidine (analogues et dérivés), Histidine (génétique), Histidine (métabolisme), Hygromycine (analogues et dérivés), Hygromycine (pharmacologie), Methyltransferases (génétique), Methyltransferases (métabolisme), Phénotype (MeSH), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Régulation de l'expression des gènes fongiques (MeSH), Saccharomyces cerevisiae (croissance et développement), Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Sirolimus (pharmacologie), Substitution d'acide aminé (MeSH), Toxine diphtérique (toxicité).
- MESH :
- analogues et dérivés : Histidine, Hygromycine.
- croissance et développement : Saccharomyces cerevisiae.
- déficit : Facteur-2 d'élongation de la chaîne peptidique.
- effets des médicaments et des substances chimiques : Biosynthèse des protéines, Division cellulaire, Saccharomyces cerevisiae.
- génétique : Facteur-1 d'élongation de la chaîne peptidique, Facteur-2 d'élongation de la chaîne peptidique, Histidine, Methyltransferases, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- métabolisme : Facteur-1 d'élongation de la chaîne peptidique, Histidine, Methyltransferases, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- pharmacologie : Anisomycine, Caféine, Cinnamates, Hygromycine, Sirolimus.
- toxicité : Toxine diphtérique.
- Délétion de gène, Phénotype, Régulation de l'expression des gènes fongiques, Substitution d'acide aminé.
English descriptors
- KwdEn :
- Amino Acid Substitution (MeSH), Anisomycin (pharmacology), Caffeine (pharmacology), Cell Division (drug effects), Cinnamates (pharmacology), Diphtheria Toxin (toxicity), Gene Deletion (MeSH), Gene Expression Regulation, Fungal (MeSH), Histidine (analogs & derivatives), Histidine (genetics), Histidine (metabolism), Hygromycin B (analogs & derivatives), Hygromycin B (pharmacology), Methyltransferases (genetics), Methyltransferases (metabolism), Peptide Elongation Factor 1 (genetics), Peptide Elongation Factor 1 (metabolism), Peptide Elongation Factor 2 (deficiency), Peptide Elongation Factor 2 (genetics), Phenotype (MeSH), Protein Biosynthesis (drug effects), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (growth & development), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Sirolimus (pharmacology).
- MESH :
- chemical , analogs & derivatives : Histidine, Hygromycin B.
- chemical , deficiency : Peptide Elongation Factor 2.
- chemical , genetics : Histidine, Methyltransferases, Peptide Elongation Factor 1, Peptide Elongation Factor 2, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Histidine, Methyltransferases, Peptide Elongation Factor 1, Saccharomyces cerevisiae Proteins.
- chemical , pharmacology : Anisomycin, Caffeine, Cinnamates, Hygromycin B, Sirolimus.
- drug effects : Cell Division, Protein Biosynthesis, Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- growth & development : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- chemical , toxicity : Diphtheria Toxin.
- Amino Acid Substitution, Gene Deletion, Gene Expression Regulation, Fungal, Phenotype.
Abstract
In eukaryotes, the modification of an invariant histidine (His-699 in yeast) residue in translation elongation factor 2 (EF2) with diphthamide involves a conserved pathway encoded by the DPH1-DPH7 gene network. Diphthamide is the target for diphtheria toxin and related lethal ADP ribosylases, which collectively kill cells by inactivating the essential translocase function of EF2 during mRNA translation and protein biosynthesis. Although this notion emphasizes the pathological importance of diphthamide, precisely why cells including our own require EF2 to carry it, is unclear. Mining the synthetic genetic array (SGA) landscape from the budding yeast Saccharomyces cerevisiae has revealed negative interactions between EF2 (EFT1-EFT2) and diphthamide (DPH1-DPH7) gene deletions. In line with these correlations, we confirm in here that loss of diphthamide modification (dphΔ) on EF2 combined with EF2 undersupply (eft2Δ) causes synthetic growth phenotypes in the composite mutant (dphΔ eft2Δ). These reflect negative interference with cell performance under standard as well as thermal and/or chemical stress conditions, cell growth rates and doubling times, competitive fitness, cell viability in the presence of TOR inhibitors (rapamycin, caffeine) and translation indicator drugs (hygromycin, anisomycin). Together with significantly suppressed tolerance towards EF2 inhibition by cytotoxic DPH5 overexpression and increased ribosomal -1 frame-shift errors in mutants lacking modifiable pools of EF2 (dphΔ, dphΔ eft2Δ), our data indicate that diphthamide is important for the fidelity of the EF2 translocation function during mRNA translation.
DOI: 10.1371/journal.pone.0205870
PubMed: 30335802
PubMed Central: PMC6193676
Affiliations:
- Allemagne
- Berlin, District de Kassel, District de Leipzig, Hesse (Land), Saxe (Land)
- Berlin, Cassel (Hesse), Leipzig
- Université technique de Berlin
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yeast.</title><author><name sortKey="Hawer, Harmen" sort="Hawer, Harmen" uniqKey="Hawer H" first="Harmen" last="Hawer">Harmen Hawer</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Biologie, Fachgebiet Mikrobiologie, Universität Kassel, Kassel, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Biologie, Fachgebiet Mikrobiologie, Universität Kassel, Kassel</wicri:regionArea><placeName><region type="land" nuts="1">Hesse (Land)</region><region type="district" nuts="2">District de Kassel</region><settlement type="city">Cassel (Hesse)</settlement></placeName></affiliation></author><author><name sortKey="Utkur, Koray" sort="Utkur, Koray" uniqKey="Utkur K" first="Koray" last="Ütkür">Koray Ütkür</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Biologie, Fachgebiet Mikrobiologie, Universität Kassel, Kassel, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Biologie, Fachgebiet Mikrobiologie, Universität Kassel, Kassel</wicri:regionArea><placeName><region type="land" nuts="1">Hesse (Land)</region><region type="district" nuts="2">District de Kassel</region><settlement type="city">Cassel (Hesse)</settlement></placeName></affiliation></author><author><name sortKey="Arend, Meike" sort="Arend, Meike" uniqKey="Arend M" first="Meike" last="Arend">Meike Arend</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Biologie, Fachgebiet Mikrobiologie, Universität Kassel, Kassel, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Biologie, Fachgebiet Mikrobiologie, Universität Kassel, Kassel</wicri:regionArea><placeName><region type="land" nuts="1">Hesse (Land)</region><region type="district" nuts="2">District de Kassel</region><settlement type="city">Cassel (Hesse)</settlement></placeName></affiliation></author><author><name sortKey="Mayer, Klaus" sort="Mayer, Klaus" uniqKey="Mayer K" first="Klaus" last="Mayer">Klaus Mayer</name><affiliation wicri:level="1"><nlm:affiliation>Roche Pharma Research & Early Development, Large Molecule Research, Roche Innovation Center München, Penzberg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Roche Pharma Research & Early Development, Large Molecule Research, Roche Innovation Center München, Penzberg</wicri:regionArea><wicri:noRegion>Penzberg</wicri:noRegion><wicri:noRegion>Penzberg</wicri:noRegion><wicri:noRegion>Penzberg</wicri:noRegion></affiliation></author><author><name sortKey="Adrian, Lorenz" sort="Adrian, Lorenz" uniqKey="Adrian L" first="Lorenz" last="Adrian">Lorenz Adrian</name><affiliation wicri:level="3"><nlm:affiliation>AG Geobiochemie, Department Isotopenbiogeochemie, Helmholtz-Zentrum für Umweltforschung GmbH-UFZ, Leipzig, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>AG Geobiochemie, Department Isotopenbiogeochemie, Helmholtz-Zentrum für Umweltforschung GmbH-UFZ, Leipzig</wicri:regionArea><placeName><region type="land" nuts="1">Saxe (Land)</region><region type="district" nuts="2">District de Leipzig</region><settlement type="city">Leipzig</settlement></placeName></affiliation><affiliation wicri:level="4"><nlm:affiliation>Fachgebiet Geobiotechnologie, Technische Universität Berlin, Berlin, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Fachgebiet Geobiotechnologie, Technische Universität Berlin, Berlin</wicri:regionArea><placeName><region type="land" nuts="3">Berlin</region><settlement type="city">Berlin</settlement></placeName><orgName type="university">Université technique de Berlin</orgName></affiliation></author><author><name sortKey="Brinkmann, Ulrich" sort="Brinkmann, Ulrich" uniqKey="Brinkmann U" first="Ulrich" last="Brinkmann">Ulrich Brinkmann</name><affiliation wicri:level="1"><nlm:affiliation>Roche Pharma Research & Early Development, Large Molecule Research, Roche Innovation Center München, Penzberg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Roche Pharma Research & Early Development, Large Molecule Research, Roche Innovation Center München, Penzberg</wicri:regionArea><wicri:noRegion>Penzberg</wicri:noRegion><wicri:noRegion>Penzberg</wicri:noRegion><wicri:noRegion>Penzberg</wicri:noRegion></affiliation></author><author><name sortKey="Schaffrath, Raffael" sort="Schaffrath, Raffael" uniqKey="Schaffrath R" first="Raffael" last="Schaffrath">Raffael Schaffrath</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Biologie, Fachgebiet Mikrobiologie, Universität Kassel, Kassel, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Biologie, Fachgebiet Mikrobiologie, Universität Kassel, Kassel</wicri:regionArea><placeName><region type="land" nuts="1">Hesse (Land)</region><region type="district" nuts="2">District de Kassel</region><settlement type="city">Cassel (Hesse)</settlement></placeName></affiliation></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Substitution (MeSH)</term><term>Anisomycin (pharmacology)</term><term>Caffeine (pharmacology)</term><term>Cell Division (drug effects)</term><term>Cinnamates (pharmacology)</term><term>Diphtheria Toxin (toxicity)</term><term>Gene Deletion (MeSH)</term><term>Gene Expression Regulation, Fungal (MeSH)</term><term>Histidine (analogs & derivatives)</term><term>Histidine (genetics)</term><term>Histidine (metabolism)</term><term>Hygromycin B (analogs & derivatives)</term><term>Hygromycin B (pharmacology)</term><term>Methyltransferases (genetics)</term><term>Methyltransferases (metabolism)</term><term>Peptide Elongation Factor 1 (genetics)</term><term>Peptide Elongation Factor 1 (metabolism)</term><term>Peptide Elongation Factor 2 (deficiency)</term><term>Peptide Elongation Factor 2 (genetics)</term><term>Phenotype (MeSH)</term><term>Protein Biosynthesis (drug effects)</term><term>Saccharomyces cerevisiae (drug effects)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (growth & development)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (genetics)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Sirolimus (pharmacology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Anisomycine (pharmacologie)</term><term>Biosynthèse des protéines (effets des médicaments et des substances chimiques)</term><term>Caféine (pharmacologie)</term><term>Cinnamates (pharmacologie)</term><term>Division cellulaire (effets des médicaments et des substances chimiques)</term><term>Délétion de gène (MeSH)</term><term>Facteur-1 d'élongation de la chaîne peptidique (génétique)</term><term>Facteur-1 d'élongation de la chaîne peptidique (métabolisme)</term><term>Facteur-2 d'élongation de la chaîne peptidique (déficit)</term><term>Facteur-2 d'élongation de la chaîne peptidique (génétique)</term><term>Histidine (analogues et dérivés)</term><term>Histidine (génétique)</term><term>Histidine (métabolisme)</term><term>Hygromycine (analogues et dérivés)</term><term>Hygromycine (pharmacologie)</term><term>Methyltransferases (génétique)</term><term>Methyltransferases (métabolisme)</term><term>Phénotype (MeSH)</term><term>Protéines de Saccharomyces cerevisiae (génétique)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Régulation de l'expression des gènes fongiques (MeSH)</term><term>Saccharomyces cerevisiae (croissance et développement)</term><term>Saccharomyces cerevisiae (effets des médicaments et des substances chimiques)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Sirolimus (pharmacologie)</term><term>Substitution d'acide aminé (MeSH)</term><term>Toxine diphtérique (toxicité)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Histidine</term><term>Hygromycin B</term></keywords><keywords scheme="MESH" type="chemical" qualifier="deficiency" xml:lang="en"><term>Peptide Elongation Factor 2</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Histidine</term><term>Methyltransferases</term><term>Peptide Elongation Factor 1</term><term>Peptide Elongation Factor 2</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Histidine</term><term>Methyltransferases</term><term>Peptide Elongation Factor 1</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Anisomycin</term><term>Caffeine</term><term>Cinnamates</term><term>Hygromycin B</term><term>Sirolimus</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Histidine</term><term>Hygromycine</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Cell Division</term><term>Protein Biosynthesis</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="déficit" xml:lang="fr"><term>Facteur-2 d'élongation de la chaîne peptidique</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Biosynthèse des protéines</term><term>Division cellulaire</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Facteur-1 d'élongation de la chaîne peptidique</term><term>Facteur-2 d'élongation de la chaîne peptidique</term><term>Histidine</term><term>Methyltransferases</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Facteur-1 d'élongation de la chaîne peptidique</term><term>Histidine</term><term>Methyltransferases</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Anisomycine</term><term>Caféine</term><term>Cinnamates</term><term>Hygromycine</term><term>Sirolimus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Diphtheria Toxin</term></keywords><keywords scheme="MESH" qualifier="toxicité" xml:lang="fr"><term>Toxine diphtérique</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Substitution</term><term>Gene Deletion</term><term>Gene Expression Regulation, Fungal</term><term>Phenotype</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Délétion de gène</term><term>Phénotype</term><term>Régulation de l'expression des gènes fongiques</term><term>Substitution d'acide aminé</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In eukaryotes, the modification of an invariant histidine (His-699 in yeast) residue in translation elongation factor 2 (EF2) with diphthamide involves a conserved pathway encoded by the DPH1-DPH7 gene network. Diphthamide is the target for diphtheria toxin and related lethal ADP ribosylases, which collectively kill cells by inactivating the essential translocase function of EF2 during mRNA translation and protein biosynthesis. Although this notion emphasizes the pathological importance of diphthamide, precisely why cells including our own require EF2 to carry it, is unclear. Mining the synthetic genetic array (SGA) landscape from the budding yeast Saccharomyces cerevisiae has revealed negative interactions between EF2 (EFT1-EFT2) and diphthamide (DPH1-DPH7) gene deletions. In line with these correlations, we confirm in here that loss of diphthamide modification (dphΔ) on EF2 combined with EF2 undersupply (eft2Δ) causes synthetic growth phenotypes in the composite mutant (dphΔ eft2Δ). These reflect negative interference with cell performance under standard as well as thermal and/or chemical stress conditions, cell growth rates and doubling times, competitive fitness, cell viability in the presence of TOR inhibitors (rapamycin, caffeine) and translation indicator drugs (hygromycin, anisomycin). Together with significantly suppressed tolerance towards EF2 inhibition by cytotoxic DPH5 overexpression and increased ribosomal -1 frame-shift errors in mutants lacking modifiable pools of EF2 (dphΔ, dphΔ eft2Δ), our data indicate that diphthamide is important for the fidelity of the EF2 translocation function during mRNA translation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30335802</PMID><DateCompleted><Year>2019</Year><Month>03</Month><Day>27</Day></DateCompleted><DateRevised><Year>2019</Year><Month>03</Month><Day>27</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>13</Volume><Issue>10</Issue><PubDate><Year>2018</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS One</ISOAbbreviation></Journal><ArticleTitle>Importance of diphthamide modified EF2 for translational accuracy and competitive cell growth in yeast.</ArticleTitle><Pagination><MedlinePgn>e0205870</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0205870</ELocationID><Abstract><AbstractText>In eukaryotes, the modification of an invariant histidine (His-699 in yeast) residue in translation elongation factor 2 (EF2) with diphthamide involves a conserved pathway encoded by the DPH1-DPH7 gene network. Diphthamide is the target for diphtheria toxin and related lethal ADP ribosylases, which collectively kill cells by inactivating the essential translocase function of EF2 during mRNA translation and protein biosynthesis. Although this notion emphasizes the pathological importance of diphthamide, precisely why cells including our own require EF2 to carry it, is unclear. Mining the synthetic genetic array (SGA) landscape from the budding yeast Saccharomyces cerevisiae has revealed negative interactions between EF2 (EFT1-EFT2) and diphthamide (DPH1-DPH7) gene deletions. In line with these correlations, we confirm in here that loss of diphthamide modification (dphΔ) on EF2 combined with EF2 undersupply (eft2Δ) causes synthetic growth phenotypes in the composite mutant (dphΔ eft2Δ). These reflect negative interference with cell performance under standard as well as thermal and/or chemical stress conditions, cell growth rates and doubling times, competitive fitness, cell viability in the presence of TOR inhibitors (rapamycin, caffeine) and translation indicator drugs (hygromycin, anisomycin). Together with significantly suppressed tolerance towards EF2 inhibition by cytotoxic DPH5 overexpression and increased ribosomal -1 frame-shift errors in mutants lacking modifiable pools of EF2 (dphΔ, dphΔ eft2Δ), our data indicate that diphthamide is important for the fidelity of the EF2 translocation function during mRNA translation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hawer</LastName><ForeName>Harmen</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Institut für Biologie, Fachgebiet Mikrobiologie, Universität Kassel, Kassel, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ütkür</LastName><ForeName>Koray</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Institut für Biologie, Fachgebiet Mikrobiologie, Universität Kassel, Kassel, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Arend</LastName><ForeName>Meike</ForeName><Initials>M</Initials><Identifier Source="ORCID">0000-0002-7561-1098</Identifier><AffiliationInfo><Affiliation>Institut für Biologie, Fachgebiet Mikrobiologie, Universität Kassel, Kassel, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mayer</LastName><ForeName>Klaus</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Roche Pharma Research & Early Development, Large Molecule Research, Roche Innovation Center München, Penzberg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Adrian</LastName><ForeName>Lorenz</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>AG Geobiochemie, Department Isotopenbiogeochemie, Helmholtz-Zentrum für Umweltforschung GmbH-UFZ, Leipzig, Germany.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Fachgebiet Geobiotechnologie, Technische Universität Berlin, Berlin, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Brinkmann</LastName><ForeName>Ulrich</ForeName><Initials>U</Initials><Identifier Source="ORCID">0000-0002-5558-0212</Identifier><AffiliationInfo><Affiliation>Roche Pharma Research & Early Development, Large Molecule Research, Roche Innovation Center München, Penzberg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Schaffrath</LastName><ForeName>Raffael</ForeName><Initials>R</Initials><Identifier Source="ORCID">0000-0001-9484-5247</Identifier><AffiliationInfo><Affiliation>Institut für Biologie, Fachgebiet Mikrobiologie, Universität Kassel, Kassel, Germany.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>10</Month><Day>18</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002934">Cinnamates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004167">Diphtheria Toxin</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020648">Peptide Elongation Factor 1</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020652">Peptide Elongation Factor 2</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>3G6A5W338E</RegistryNumber><NameOfSubstance UI="D002110">Caffeine</NameOfSubstance></Chemical><Chemical><RegistryNumber>3XQ2233B0B</RegistryNumber><NameOfSubstance UI="D006921">Hygromycin B</NameOfSubstance></Chemical><Chemical><RegistryNumber>3YJY415DDI</RegistryNumber><NameOfSubstance UI="C026273">hygromycin A</NameOfSubstance></Chemical><Chemical><RegistryNumber>4QD397987E</RegistryNumber><NameOfSubstance UI="D006639">Histidine</NameOfSubstance></Chemical><Chemical><RegistryNumber>6C74YM2NGI</RegistryNumber><NameOfSubstance UI="D000841">Anisomycin</NameOfSubstance></Chemical><Chemical><RegistryNumber>75645-22-6</RegistryNumber><NameOfSubstance UI="C027527">diphthamide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber><NameOfSubstance UI="D008780">Methyltransferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.98</RegistryNumber><NameOfSubstance UI="C076235">DPH5 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber><NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D019943" MajorTopicYN="N">Amino Acid Substitution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000841" MajorTopicYN="N">Anisomycin</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002110" MajorTopicYN="N">Caffeine</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002455" MajorTopicYN="N">Cell Division</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002934" MajorTopicYN="N">Cinnamates</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004167" MajorTopicYN="N">Diphtheria Toxin</DescriptorName><QualifierName UI="Q000633" MajorTopicYN="N">toxicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017353" MajorTopicYN="N">Gene Deletion</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="Y">Gene Expression Regulation, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006639" MajorTopicYN="N">Histidine</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006921" MajorTopicYN="N">Hygromycin B</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008780" MajorTopicYN="N">Methyltransferases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020648" MajorTopicYN="N">Peptide Elongation Factor 1</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020652" MajorTopicYN="N">Peptide Elongation Factor 2</DescriptorName><QualifierName UI="Q000172" MajorTopicYN="N">deficiency</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010641" MajorTopicYN="N">Phenotype</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014176" MajorTopicYN="N">Protein Biosynthesis</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020123" MajorTopicYN="N">Sirolimus</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading></MeshHeadingList><CoiStatement>KM and UB are employed by and members of Roche Pharma Research & Early Development. Roche is interested in targeted therapies and diagnostics. This does not alter our adherence to PLOS ONE policies on sharing data and materials. All other authors (HH, KÜ, MA, LA and RS) have declared that no competing interests exist.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>08</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>10</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>10</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>10</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>3</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">30335802</ArticleId><ArticleId IdType="doi">10.1371/journal.pone.0205870</ArticleId><ArticleId IdType="pii">PONE-D-18-23186</ArticleId><ArticleId 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Kassel</li><li>District de Leipzig</li><li>Hesse (Land)</li><li>Saxe (Land)</li></region><settlement><li>Berlin</li><li>Cassel (Hesse)</li><li>Leipzig</li></settlement><orgName><li>Université technique de Berlin</li></orgName></list><tree><country name="Allemagne"><region name="Hesse (Land)"><name sortKey="Hawer, Harmen" sort="Hawer, Harmen" uniqKey="Hawer H" first="Harmen" last="Hawer">Harmen Hawer</name></region><name sortKey="Adrian, Lorenz" sort="Adrian, Lorenz" uniqKey="Adrian L" first="Lorenz" last="Adrian">Lorenz Adrian</name><name sortKey="Adrian, Lorenz" sort="Adrian, Lorenz" uniqKey="Adrian L" first="Lorenz" last="Adrian">Lorenz Adrian</name><name sortKey="Arend, Meike" sort="Arend, Meike" uniqKey="Arend M" first="Meike" last="Arend">Meike Arend</name><name sortKey="Brinkmann, Ulrich" sort="Brinkmann, Ulrich" uniqKey="Brinkmann U" first="Ulrich" last="Brinkmann">Ulrich Brinkmann</name><name sortKey="Mayer, Klaus" sort="Mayer, Klaus" uniqKey="Mayer K" first="Klaus" last="Mayer">Klaus Mayer</name><name sortKey="Schaffrath, Raffael" sort="Schaffrath, Raffael" uniqKey="Schaffrath R" first="Raffael" last="Schaffrath">Raffael Schaffrath</name><name sortKey="Utkur, Koray" sort="Utkur, Koray" uniqKey="Utkur K" first="Koray" last="Ütkür">Koray Ütkür</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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