RapamycinFungusV1, Main, Exploration, bibRecord, 000B88

The yeast ζ-crystallin/NADPH:quinone oxidoreductase (Zta1p) is under nutritional control by the target of rapamycin pathway and is involved in the regulation of argininosuccinate lyase mRNA half-life.

Identifieur interne : 000B88 ( Main/Exploration ); précédent : 000B87; suivant : 000B89

The yeast ζ-crystallin/NADPH:quinone oxidoreductase (Zta1p) is under nutritional control by the target of rapamycin pathway and is involved in the regulation of argininosuccinate lyase mRNA half-life.

Auteurs : Eva Crosas [Espagne] ; Lauro Sumoy [Espagne] ; Eva González [Espagne] ; Maykelis Díaz [Espagne] ; Salvador Bartolomé [Espagne] ; Jaume Farrés [Espagne] ; Xavier Parés [Espagne] ; Josep Antoni Biosca [Espagne] ; María Rosario Fernández [Espagne]

Source :

The FEBS journal [ 1742-4658 ] ; 2015.

RBID : pubmed:25715111

Descripteurs français

English descriptors

KwdEn :
- Argininosuccinate Lyase (metabolism), DNA (metabolism), Galactokinase (metabolism), NADP (metabolism), Quinone Reductases (genetics), Quinone Reductases (metabolism), RNA (metabolism), Real-Time Polymerase Chain Reaction (MeSH), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (metabolism), zeta-Crystallins (genetics), zeta-Crystallins (metabolism).
MESH :
- chemical , genetics : Quinone Reductases, zeta-Crystallins.
- chemical , metabolism : Argininosuccinate Lyase, DNA, Galactokinase, NADP, Quinone Reductases, RNA, Saccharomyces cerevisiae Proteins, zeta-Crystallins.
- metabolism : Saccharomyces cerevisiae.
- Real-Time Polymerase Chain Reaction.

Abstract

The yeast ζ-crystallin (Zta1p) is a quinone oxidoreductase belonging to the ζ-crystallin family, with activity in the reduction of alkenal/alkenone compounds. Various biological functions have been ascribed to the members of this protein family, such as their ability to interact specifically with AU-rich sequences in mRNA, and thus they have been proposed to act as AU-rich element-binding proteins (AREBPs). In this study, we evaluated the specificity of Zta1p for RNA versus DNA by means of a novel nonisotopic method for the in vitro quantitative detection of protein · RNA complexes. Through comparative transcriptomic analysis, we found that the lack of Zta1p negatively affects the expression of a group of genes involved in amino acid biosynthesis, the argininosuccinate lyase (ARG4) gene being one of them. Here, we propose that Zta1p participates in the post-transcriptional regulation of ARG4 expression by increasing the ARG4 mRNA half-life. In addition, expression of the ζ-crystallin gene (ZTA1) is itself regulated by nutrient availability through the general amino acid control and target of rapamycin pathways. Our results shed new light on the ζ-crystallin family members from yeast to humans as stress response proteins with a bifunctional role in the detoxification of alkenal and alkenone compounds, and the regulation of gene expression.

DOI: 10.1111/febs.13246
PubMed: 25715111

Affiliations:

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Le document en format XML

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<term>Quinone Reductases (metabolism)</term>
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<term>Real-Time Polymerase Chain Reaction (MeSH)</term>
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<term>Galactokinase (métabolisme)</term>
<term>NADP (métabolisme)</term>
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<term>Quinone reductases (métabolisme)</term>
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<term>NADP</term>
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<front><div type="abstract" xml:lang="en">The yeast ζ-crystallin (Zta1p) is a quinone oxidoreductase belonging to the ζ-crystallin family, with activity in the reduction of alkenal/alkenone compounds. Various biological functions have been ascribed to the members of this protein family, such as their ability to interact specifically with AU-rich sequences in mRNA, and thus they have been proposed to act as AU-rich element-binding proteins (AREBPs). In this study, we evaluated the specificity of Zta1p for RNA versus DNA by means of a novel nonisotopic method for the in vitro quantitative detection of protein · RNA complexes. Through comparative transcriptomic analysis, we found that the lack of Zta1p negatively affects the expression of a group of genes involved in amino acid biosynthesis, the argininosuccinate lyase (ARG4) gene being one of them. Here, we propose that Zta1p participates in the post-transcriptional regulation of ARG4 expression by increasing the ARG4 mRNA half-life. In addition, expression of the ζ-crystallin gene (ZTA1) is itself regulated by nutrient availability through the general amino acid control and target of rapamycin pathways. Our results shed new light on the ζ-crystallin family members from yeast to humans as stress response proteins with a bifunctional role in the detoxification of alkenal and alkenone compounds, and the regulation of gene expression.</div>
</front>
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<Abstract><AbstractText>The yeast ζ-crystallin (Zta1p) is a quinone oxidoreductase belonging to the ζ-crystallin family, with activity in the reduction of alkenal/alkenone compounds. Various biological functions have been ascribed to the members of this protein family, such as their ability to interact specifically with AU-rich sequences in mRNA, and thus they have been proposed to act as AU-rich element-binding proteins (AREBPs). In this study, we evaluated the specificity of Zta1p for RNA versus DNA by means of a novel nonisotopic method for the in vitro quantitative detection of protein · RNA complexes. Through comparative transcriptomic analysis, we found that the lack of Zta1p negatively affects the expression of a group of genes involved in amino acid biosynthesis, the argininosuccinate lyase (ARG4) gene being one of them. Here, we propose that Zta1p participates in the post-transcriptional regulation of ARG4 expression by increasing the ARG4 mRNA half-life. In addition, expression of the ζ-crystallin gene (ZTA1) is itself regulated by nutrient availability through the general amino acid control and target of rapamycin pathways. Our results shed new light on the ζ-crystallin family members from yeast to humans as stress response proteins with a bifunctional role in the detoxification of alkenal and alkenone compounds, and the regulation of gene expression.</AbstractText>
<CopyrightInformation>© 2015 FEBS.</CopyrightInformation>
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<ForeName>Eva</ForeName>
<Initials>E</Initials>
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<AffiliationInfo><Affiliation>Microarray Unit, Genomics Core Facility, Center for Genomic Regulation (CRG) - Universitat Pompeu Fabra (UPF), Barcelona, Spain.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Institut de Medicina Predictiva i Personalitzada del Càncer, IGTP, Campus Can Ruti, Badalona, Barcelona, Spain.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>González</LastName>
<ForeName>Eva</ForeName>
<Initials>E</Initials>
<AffiliationInfo><Affiliation>Microarray Unit, Genomics Core Facility, Center for Genomic Regulation (CRG) - Universitat Pompeu Fabra (UPF), Barcelona, Spain.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Díaz</LastName>
<ForeName>Maykelis</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Spain.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Bartolomé</LastName>
<ForeName>Salvador</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Laboratory of Luminescence and Spectroscopy of Biomolecules (LLEB), Universitat Autònoma de Barcelona, Spain.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Farrés</LastName>
<ForeName>Jaume</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Spain.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Parés</LastName>
<ForeName>Xavier</ForeName>
<Initials>X</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Spain.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Biosca</LastName>
<ForeName>Josep Antoni</ForeName>
<Initials>JA</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Spain.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Fernández</LastName>
<ForeName>María Rosario</ForeName>
<Initials>MR</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Spain.</Affiliation>
</AffiliationInfo>
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<Month>03</Month>
<Day>18</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>FEBS J</MedlineTA>
<NlmUniqueID>101229646</NlmUniqueID>
<ISSNLinking>1742-464X</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D038226">zeta-Crystallins</NameOfSubstance>
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<Chemical><RegistryNumber>53-59-8</RegistryNumber>
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<Chemical><RegistryNumber>EC 1.6.99.-</RegistryNumber>
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<Chemical><RegistryNumber>EC 2.7.1.6</RegistryNumber>
<NameOfSubstance UI="C524219">GAL1 protein, S cerevisiae</NameOfSubstance>
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<Chemical><RegistryNumber>EC 2.7.1.6</RegistryNumber>
<NameOfSubstance UI="D005686">Galactokinase</NameOfSubstance>
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<Chemical><RegistryNumber>EC 4.3.2.1</RegistryNumber>
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<Chemical><RegistryNumber>EC 4.3.2.1</RegistryNumber>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D001123" MajorTopicYN="N">Argininosuccinate Lyase</DescriptorName>
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<MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D038226" MajorTopicYN="N">zeta-Crystallins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">AU-rich binding protein</Keyword>
<Keyword MajorTopicYN="N">amino acid starvation</Keyword>
<Keyword MajorTopicYN="N">argininosuccinate lyase</Keyword>
<Keyword MajorTopicYN="N">crystallins</Keyword>
<Keyword MajorTopicYN="N">medium-chain dehydrogenase/reductase</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year>
<Month>04</Month>
<Day>22</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2015</Year>
<Month>01</Month>
<Day>28</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2015</Year>
<Month>02</Month>
<Day>19</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2015</Year>
<Month>2</Month>
<Day>26</Day>
<Hour>6</Hour>
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<Day>26</Day>
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<PubMedPubDate PubStatus="medline"><Year>2015</Year>
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<ArticleIdList><ArticleId IdType="pubmed">25715111</ArticleId>
<ArticleId IdType="doi">10.1111/febs.13246</ArticleId>
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<affiliations><list><country><li>Espagne</li>
</country>
<region><li>Catalogne</li>
</region>
<settlement><li>Barcelone</li>
</settlement>
<orgName><li>Université autonome de Barcelone</li>
</orgName>
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<tree><country name="Espagne"><region name="Catalogne"><name sortKey="Crosas, Eva" sort="Crosas, Eva" uniqKey="Crosas E" first="Eva" last="Crosas">Eva Crosas</name>
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<name sortKey="Bartolome, Salvador" sort="Bartolome, Salvador" uniqKey="Bartolome S" first="Salvador" last="Bartolomé">Salvador Bartolomé</name>
<name sortKey="Biosca, Josep Antoni" sort="Biosca, Josep Antoni" uniqKey="Biosca J" first="Josep Antoni" last="Biosca">Josep Antoni Biosca</name>
<name sortKey="Crosas, Eva" sort="Crosas, Eva" uniqKey="Crosas E" first="Eva" last="Crosas">Eva Crosas</name>
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   |texte=   The yeast ζ-crystallin/NADPH:quinone oxidoreductase (Zta1p) is under nutritional control by the target of rapamycin pathway and is involved in the regulation of argininosuccinate lyase mRNA half-life.
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The yeast ζ-crystallin/NADPH:quinone oxidoreductase (Zta1p) is under nutritional control by the target of rapamycin pathway and is involved in the regulation of argininosuccinate lyase mRNA half-life.

The yeast ζ-crystallin/NADPH:quinone oxidoreductase (Zta1p) is under nutritional control by the target of rapamycin pathway and is involved in the regulation of argininosuccinate lyase mRNA half-life.

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