RapamycinFungusV1, Main, Exploration, bibRecord, 000257

Protein Methylation and Translation: Role of Lysine Modification on the Function of Yeast Elongation Factor 1A.

Identifieur interne : 000257 ( Main/Exploration ); précédent : 000256; suivant : 000258

Protein Methylation and Translation: Role of Lysine Modification on the Function of Yeast Elongation Factor 1A.

Auteurs : Jonelle T. White [États-Unis] ; Tieranee Cato [États-Unis] ; Neil Deramchi [États-Unis] ; Jason Gabunilas [États-Unis] ; Kevin R. Roy [États-Unis] ; Charles Wang [États-Unis] ; Guillaume F. Chanfreau [États-Unis] ; Steven G. Clarke [États-Unis]

Source :

Biochemistry [ 1520-4995 ] ; 2019.

RBID : pubmed:31738538

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Motifs (MeSH), Lysine (metabolism), Methylation (MeSH), Methyltransferases (genetics), Methyltransferases (metabolism), Peptide Elongation Factor 1 (chemistry), Peptide Elongation Factor 1 (metabolism), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism).
MESH :
- chemical , chemistry : Peptide Elongation Factor 1, Saccharomyces cerevisiae Proteins.
- chemical , genetics : Methyltransferases, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Lysine, Methyltransferases, Peptide Elongation Factor 1, Saccharomyces cerevisiae Proteins.
- enzymology : Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Amino Acid Motifs, Methylation.

Abstract

To date, 12 protein lysine methyltransferases that modify translational elongation factors and ribosomal proteins (Efm1-7 and Rkm 1-5) have been identified in the yeast Saccharomyces cerevisiae. Of these 12, five (Efm1 and Efm4-7) appear to be specific to elongation factor 1A (EF1A), the protein responsible for bringing aminoacyl-tRNAs to the ribosome. In S. cerevisiae, the functional implications of lysine methylation in translation are mostly unknown. In this work, we assessed the physiological impact of disrupting EF1A methylation in a strain where four of the most conserved methylated lysine sites are mutated to arginine residues and in strains lacking either four or five of the Efm lysine methyltransferases specific to EF1A. We found that loss of EF1A methylation was not lethal but resulted in reduced growth rates, particularly under caffeine and rapamycin stress conditions, suggesting EF1A interacts with the TORC1 pathway, as well as altered sensitivities to ribosomal inhibitors. We also detected reduced cellular levels of the EF1A protein, which surprisingly was not reflected in its stability in vivo. We present evidence that these Efm methyltransferases appear to be largely devoted to the modification of EF1A, finding no evidence of the methylation of other substrates in the yeast cell. This work starts to illuminate why one protein can need five different methyltransferases for its functions and highlights the resilience of yeast to alterations in their posttranslational modifications.

DOI: 10.1021/acs.biochem.9b00818
PubMed: 31738538
PubMed Central: PMC6913935

Affiliations:

États-Unis

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<series><title level="j">Biochemistry</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs (MeSH)</term>
<term>Lysine (metabolism)</term>
<term>Methylation (MeSH)</term>
<term>Methyltransferases (genetics)</term>
<term>Methyltransferases (metabolism)</term>
<term>Peptide Elongation Factor 1 (chemistry)</term>
<term>Peptide Elongation Factor 1 (metabolism)</term>
<term>Saccharomyces cerevisiae (enzymology)</term>
<term>Saccharomyces cerevisiae (genetics)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (chemistry)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Facteur-1 d'élongation de la chaîne peptidique (composition chimique)</term>
<term>Facteur-1 d'élongation de la chaîne peptidique (métabolisme)</term>
<term>Lysine (métabolisme)</term>
<term>Methyltransferases (génétique)</term>
<term>Methyltransferases (métabolisme)</term>
<term>Motifs d'acides aminés (MeSH)</term>
<term>Méthylation (MeSH)</term>
<term>Protéines de Saccharomyces cerevisiae (composition chimique)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Saccharomyces cerevisiae (enzymologie)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peptide Elongation Factor 1</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Methyltransferases</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lysine</term>
<term>Methyltransferases</term>
<term>Peptide Elongation Factor 1</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Facteur-1 d'élongation de la chaîne peptidique</term>
<term>Protéines de Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><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>Lysine</term>
<term>Methyltransferases</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term>
<term>Methylation</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Motifs d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">To date, 12 protein lysine methyltransferases that modify translational elongation factors and ribosomal proteins (Efm1-7 and Rkm 1-5) have been identified in the yeast <i>Saccharomyces cerevisiae</i>
. Of these 12, five (Efm1 and Efm4-7) appear to be specific to elongation factor 1A (EF1A), the protein responsible for bringing aminoacyl-tRNAs to the ribosome. In <i>S</i>
. <i>cerevisiae</i>
, the functional implications of lysine methylation in translation are mostly unknown. In this work, we assessed the physiological impact of disrupting EF1A methylation in a strain where four of the most conserved methylated lysine sites are mutated to arginine residues and in strains lacking either four or five of the Efm lysine methyltransferases specific to EF1A. We found that loss of EF1A methylation was not lethal but resulted in reduced growth rates, particularly under caffeine and rapamycin stress conditions, suggesting EF1A interacts with the TORC1 pathway, as well as altered sensitivities to ribosomal inhibitors. We also detected reduced cellular levels of the EF1A protein, which surprisingly was not reflected in its stability <i>in vivo</i>
. We present evidence that these Efm methyltransferases appear to be largely devoted to the modification of EF1A, finding no evidence of the methylation of other substrates in the yeast cell. This work starts to illuminate why one protein can need five different methyltransferases for its functions and highlights the resilience of yeast to alterations in their posttranslational modifications.</div>
</front>
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<Month>06</Month>
<Day>29</Day>
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<Day>29</Day>
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<Title>Biochemistry</Title>
<ISOAbbreviation>Biochemistry</ISOAbbreviation>
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<ArticleTitle>Protein Methylation and Translation: Role of Lysine Modification on the Function of Yeast Elongation Factor 1A.</ArticleTitle>
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</Pagination>
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<Abstract><AbstractText>To date, 12 protein lysine methyltransferases that modify translational elongation factors and ribosomal proteins (Efm1-7 and Rkm 1-5) have been identified in the yeast <i>Saccharomyces cerevisiae</i>
. Of these 12, five (Efm1 and Efm4-7) appear to be specific to elongation factor 1A (EF1A), the protein responsible for bringing aminoacyl-tRNAs to the ribosome. In <i>S</i>
. <i>cerevisiae</i>
, the functional implications of lysine methylation in translation are mostly unknown. In this work, we assessed the physiological impact of disrupting EF1A methylation in a strain where four of the most conserved methylated lysine sites are mutated to arginine residues and in strains lacking either four or five of the Efm lysine methyltransferases specific to EF1A. We found that loss of EF1A methylation was not lethal but resulted in reduced growth rates, particularly under caffeine and rapamycin stress conditions, suggesting EF1A interacts with the TORC1 pathway, as well as altered sensitivities to ribosomal inhibitors. We also detected reduced cellular levels of the EF1A protein, which surprisingly was not reflected in its stability <i>in vivo</i>
. We present evidence that these Efm methyltransferases appear to be largely devoted to the modification of EF1A, finding no evidence of the methylation of other substrates in the yeast cell. This work starts to illuminate why one protein can need five different methyltransferases for its functions and highlights the resilience of yeast to alterations in their posttranslational modifications.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>White</LastName>
<ForeName>Jonelle T</ForeName>
<Initials>JT</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry and Molecular Biology Institute , University of California, Los Angeles , Los Angeles , California 90095 , United States.</Affiliation>
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<ForeName>Tieranee</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry and Molecular Biology Institute , University of California, Los Angeles , Los Angeles , California 90095 , United States.</Affiliation>
</AffiliationInfo>
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<ForeName>Neil</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry and Molecular Biology Institute , University of California, Los Angeles , Los Angeles , California 90095 , United States.</Affiliation>
</AffiliationInfo>
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<ForeName>Jason</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry and Molecular Biology Institute , University of California, Los Angeles , Los Angeles , California 90095 , United States.</Affiliation>
</AffiliationInfo>
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<ForeName>Kevin R</ForeName>
<Initials>KR</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry and Molecular Biology Institute , University of California, Los Angeles , Los Angeles , California 90095 , United States.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Charles</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry and Molecular Biology Institute , University of California, Los Angeles , Los Angeles , California 90095 , United States.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Chanfreau</LastName>
<ForeName>Guillaume F</ForeName>
<Initials>GF</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry and Molecular Biology Institute , University of California, Los Angeles , Los Angeles , California 90095 , United States.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Clarke</LastName>
<ForeName>Steven G</ForeName>
<Initials>SG</Initials>
<Identifier Source="ORCID">0000-0002-7303-6632</Identifier>
<AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry and Molecular Biology Institute , University of California, Los Angeles , Los Angeles , California 90095 , United States.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>R35 GM130370</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>T32 GM007185</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
</GrantList>
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<PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
<PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2019</Year>
<Month>12</Month>
<Day>02</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Biochemistry</MedlineTA>
<NlmUniqueID>0370623</NlmUniqueID>
<ISSNLinking>0006-2960</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D020648">Peptide Elongation Factor 1</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C410826">TEF1 protein, S cerevisiae</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber>
<NameOfSubstance UI="C000607381">Efm6 protein, S cerevisiae</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber>
<NameOfSubstance UI="D008780">Methyltransferases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>K3Z4F929H6</RegistryNumber>
<NameOfSubstance UI="D008239">Lysine</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
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Protein Methylation and Translation: Role of Lysine Modification on the Function of Yeast Elongation Factor 1A.

Protein Methylation and Translation: Role of Lysine Modification on the Function of Yeast Elongation Factor 1A.

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