Demonstration of translation elongation factor 3 activity from a non-fungal species, Phytophthora infestans.
Identifieur interne : 000808 ( Main/Exploration ); précédent : 000807; suivant : 000809Demonstration of translation elongation factor 3 activity from a non-fungal species, Phytophthora infestans.
Auteurs : Maria K. Mateyak [États-Unis] ; Justyna K. Pupek [États-Unis] ; Alexandra E. Garino [États-Unis] ; Mccllelan C. Knapp [États-Unis] ; Sarah F. Colmer [États-Unis] ; Terri Goss Kinzy [États-Unis] ; Stephen Dunaway [États-Unis]Source :
- PloS one [ 1932-6203 ] ; 2018.
Descripteurs français
- KwdFr :
- MESH :
- classification : Facteurs élongation chaîne peptidique.
- métabolisme : Facteurs élongation chaîne peptidique, Phytophthora infestans.
- Phylogenèse, Élongation de la traduction.
English descriptors
- KwdEn :
- MESH :
- chemical , classification : Peptide Elongation Factors.
- chemical , metabolism : Peptide Elongation Factors.
- metabolism : Phytophthora infestans.
- Peptide Chain Elongation, Translational, Phylogeny.
Abstract
In most eukaryotic organisms, translation elongation requires two highly conserved elongation factors eEF1A and eEF2. Fungal systems are unique in requiring a third factor, the eukaryotic Elongation Factor 3 (eEF3). For decades, eEF3, a ribosome-dependent ATPase, was considered "fungal-specific", however, recent bioinformatics analysis indicates it may be more widely distributed among other unicellular eukaryotes. In order to determine whether divergent eEF3-like proteins from other eukaryotic organisms can provide the essential functions of eEF3 in budding yeast, the eEF3-like proteins from Schizosaccharomyes pombe and an oomycete, Phytophthora infestans, were cloned and expressed in Saccharomyces cerevisiae. Plasmid shuffling experiments showed that both S. pombe and P. infestans eEF3 can support the growth of S. cerevisiae in the absence of endogenous budding yeast eEF3. Consistent with its ability to provide the essential functions of eEF3, P. infestans eEF3 possessed ribosome-dependent ATPase activity. Yeast cells expressing P. infestans eEF3 displayed reduced protein synthesis due to defects in translation elongation/termination. Identification of eEF3 in divergent species will advance understanding of its function and the ribosome specific determinants that lead to its requirement as well as contribute to the identification of functional domains of eEF3 for potential drug discovery.
DOI: 10.1371/journal.pone.0190524
PubMed: 29300771
PubMed Central: PMC5754060
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Mateyak</name><affiliation wicri:level="2"><nlm:affiliation>Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Rutgers, the State University of New Jersey, Piscataway, NJ, United States of America.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Rutgers, the State University of New Jersey, Piscataway, NJ</wicri:regionArea><placeName><region type="state">New Jersey</region></placeName></affiliation></author><author><name sortKey="Pupek, Justyna K" sort="Pupek, Justyna K" uniqKey="Pupek J" first="Justyna K" last="Pupek">Justyna K. 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Garino</name><affiliation wicri:level="2"><nlm:affiliation>Department of Biology, Drew University, Madison, NJ, United States of America.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biology, Drew University, Madison, NJ</wicri:regionArea><placeName><region type="state">New Jersey</region></placeName></affiliation></author><author><name sortKey="Knapp, Mccllelan C" sort="Knapp, Mccllelan C" uniqKey="Knapp M" first="Mccllelan C" last="Knapp">Mccllelan C. Knapp</name><affiliation wicri:level="2"><nlm:affiliation>Department of Biology, Drew University, Madison, NJ, United States of America.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biology, Drew University, Madison, NJ</wicri:regionArea><placeName><region type="state">New Jersey</region></placeName></affiliation></author><author><name sortKey="Colmer, Sarah F" sort="Colmer, Sarah F" uniqKey="Colmer S" first="Sarah F" last="Colmer">Sarah F. Colmer</name><affiliation wicri:level="2"><nlm:affiliation>Department of Biology, Drew University, Madison, NJ, United States of America.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biology, Drew University, Madison, NJ</wicri:regionArea><placeName><region type="state">New Jersey</region></placeName></affiliation></author><author><name sortKey="Kinzy, Terri Goss" sort="Kinzy, Terri Goss" uniqKey="Kinzy T" first="Terri Goss" last="Kinzy">Terri Goss Kinzy</name><affiliation wicri:level="2"><nlm:affiliation>Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Rutgers, the State University of New Jersey, Piscataway, NJ, United States of America.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Rutgers, the State University of New Jersey, Piscataway, NJ</wicri:regionArea><placeName><region type="state">New Jersey</region></placeName></affiliation></author><author><name sortKey="Dunaway, Stephen" sort="Dunaway, Stephen" uniqKey="Dunaway S" first="Stephen" last="Dunaway">Stephen Dunaway</name><affiliation wicri:level="2"><nlm:affiliation>Department of Biology, Drew University, Madison, NJ, United States of America.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biology, Drew University, Madison, NJ</wicri:regionArea><placeName><region type="state">New Jersey</region></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>Peptide Chain Elongation, Translational (MeSH)</term><term>Peptide Elongation Factors (classification)</term><term>Peptide Elongation Factors (metabolism)</term><term>Phylogeny (MeSH)</term><term>Phytophthora infestans (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Facteurs élongation chaîne peptidique (classification)</term><term>Facteurs élongation chaîne peptidique (métabolisme)</term><term>Phylogenèse (MeSH)</term><term>Phytophthora infestans (métabolisme)</term><term>Élongation de la traduction (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="classification" xml:lang="en"><term>Peptide Elongation Factors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peptide Elongation Factors</term></keywords><keywords scheme="MESH" qualifier="classification" xml:lang="fr"><term>Facteurs élongation chaîne peptidique</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Phytophthora infestans</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Facteurs élongation chaîne peptidique</term><term>Phytophthora infestans</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Peptide Chain Elongation, Translational</term><term>Phylogeny</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Phylogenèse</term><term>Élongation de la traduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In most eukaryotic organisms, translation elongation requires two highly conserved elongation factors eEF1A and eEF2. Fungal systems are unique in requiring a third factor, the eukaryotic Elongation Factor 3 (eEF3). For decades, eEF3, a ribosome-dependent ATPase, was considered "fungal-specific", however, recent bioinformatics analysis indicates it may be more widely distributed among other unicellular eukaryotes. In order to determine whether divergent eEF3-like proteins from other eukaryotic organisms can provide the essential functions of eEF3 in budding yeast, the eEF3-like proteins from Schizosaccharomyes pombe and an oomycete, Phytophthora infestans, were cloned and expressed in Saccharomyces cerevisiae. Plasmid shuffling experiments showed that both S. pombe and P. infestans eEF3 can support the growth of S. cerevisiae in the absence of endogenous budding yeast eEF3. Consistent with its ability to provide the essential functions of eEF3, P. infestans eEF3 possessed ribosome-dependent ATPase activity. Yeast cells expressing P. infestans eEF3 displayed reduced protein synthesis due to defects in translation elongation/termination. Identification of eEF3 in divergent species will advance understanding of its function and the ribosome specific determinants that lead to its requirement as well as contribute to the identification of functional domains of eEF3 for potential drug discovery.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29300771</PMID><DateCompleted><Year>2018</Year><Month>02</Month><Day>15</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>13</Volume><Issue>1</Issue><PubDate><Year>2018</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS One</ISOAbbreviation></Journal><ArticleTitle>Demonstration of translation elongation factor 3 activity from a non-fungal species, Phytophthora infestans.</ArticleTitle><Pagination><MedlinePgn>e0190524</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0190524</ELocationID><Abstract><AbstractText>In most eukaryotic organisms, translation elongation requires two highly conserved elongation factors eEF1A and eEF2. Fungal systems are unique in requiring a third factor, the eukaryotic Elongation Factor 3 (eEF3). For decades, eEF3, a ribosome-dependent ATPase, was considered "fungal-specific", however, recent bioinformatics analysis indicates it may be more widely distributed among other unicellular eukaryotes. In order to determine whether divergent eEF3-like proteins from other eukaryotic organisms can provide the essential functions of eEF3 in budding yeast, the eEF3-like proteins from Schizosaccharomyes pombe and an oomycete, Phytophthora infestans, were cloned and expressed in Saccharomyces cerevisiae. Plasmid shuffling experiments showed that both S. pombe and P. infestans eEF3 can support the growth of S. cerevisiae in the absence of endogenous budding yeast eEF3. Consistent with its ability to provide the essential functions of eEF3, P. infestans eEF3 possessed ribosome-dependent ATPase activity. Yeast cells expressing P. infestans eEF3 displayed reduced protein synthesis due to defects in translation elongation/termination. Identification of eEF3 in divergent species will advance understanding of its function and the ribosome specific determinants that lead to its requirement as well as contribute to the identification of functional domains of eEF3 for potential drug discovery.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Mateyak</LastName><ForeName>Maria K</ForeName><Initials>MK</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Rutgers, the State University of New Jersey, Piscataway, NJ, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pupek</LastName><ForeName>Justyna K</ForeName><Initials>JK</Initials><AffiliationInfo><Affiliation>Department of Biology, Drew University, Madison, NJ, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Garino</LastName><ForeName>Alexandra E</ForeName><Initials>AE</Initials><AffiliationInfo><Affiliation>Department of Biology, Drew University, Madison, NJ, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Knapp</LastName><ForeName>McCllelan C</ForeName><Initials>MC</Initials><AffiliationInfo><Affiliation>Department of Biology, Drew University, Madison, NJ, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Colmer</LastName><ForeName>Sarah F</ForeName><Initials>SF</Initials><AffiliationInfo><Affiliation>Department of Biology, Drew University, Madison, NJ, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kinzy</LastName><ForeName>Terri Goss</ForeName><Initials>TG</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Rutgers, the State University of New Jersey, Piscataway, NJ, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dunaway</LastName><ForeName>Stephen</ForeName><Initials>S</Initials><Identifier Source="ORCID">0000-0001-6580-4737</Identifier><AffiliationInfo><Affiliation>Department of Biology, Drew University, Madison, NJ, United States of America.</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>01</Month><Day>04</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="D010445">Peptide Elongation Factors</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D010441" MajorTopicYN="N">Peptide Chain Elongation, Translational</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010445" MajorTopicYN="N">Peptide Elongation Factors</DescriptorName><QualifierName UI="Q000145" MajorTopicYN="N">classification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055750" MajorTopicYN="N">Phytophthora infestans</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year><Month>09</Month><Day>22</Day></PubMedPubDate><PubMedPubDate 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