Yeast thioredoxin reductase Trr1p controls TORC1-regulated processes.
Identifieur interne : 000427 ( Main/Exploration ); précédent : 000426; suivant : 000428Yeast thioredoxin reductase Trr1p controls TORC1-regulated processes.
Auteurs : Cecilia Picazo [Espagne] ; Emilia Matallana [Espagne] ; Agustín Aranda [Espagne]Source :
- Scientific reports [ 2045-2322 ] ; 2018.
Descripteurs français
- KwdFr :
- MESH :
- génétique : Levures, Thioredoxin reductase 1.
- métabolisme : Acides aminés, Antioxydants, Complexe-1 cible mécanistique de la rapamycine, Levures, Thioredoxin reductase 1.
- Délétion de gène, Transduction du signal.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Thioredoxin Reductase 1.
- chemical , metabolism : Amino Acids, Antioxidants, Mechanistic Target of Rapamycin Complex 1, Thioredoxin Reductase 1.
- genetics : Yeasts.
- metabolism : Yeasts.
- Gene Deletion, Signal Transduction.
Abstract
The thioredoxin system plays a predominant role in the control of cellular redox status. Thioredoxin reductase fuels the system with reducing power in the form of NADPH. The TORC1 complex promotes growth and protein synthesis when nutrients, particularly amino acids, are abundant. It also represses catabolic processes, like autophagy, which are activated during starvation. We analyzed the impact of yeast cytosolic thioredoxin reductase TRR1 deletion under different environmental conditions. It shortens chronological life span and reduces growth in grape juice fermentation. TRR1 deletion has a global impact on metabolism during fermentation. As expected, it reduces oxidative stress tolerance, but a compensatory response is triggered, with catalase and glutathione increasing. Unexpectedly, TRR1 deletion causes sensitivity to the inhibitors of the TORC1 pathway, such as rapamycin. This correlates with low Tor2p kinase levels and indicates a direct role of Trr1p in its stability. Markers of TORC1 activity, however, suggest increased TORC1 activity. The autophagy caused by nitrogen starvation is reduced in the trr1Δ mutant. Ribosomal protein Rsp6p is dephosphorylated in the presence of rapamycin. This dephosphorylation diminishes in the TRR1 deletion strain. These results show a complex network of interactions between thioredoxin reductase Trr1p and the processes controlled by TOR.
DOI: 10.1038/s41598-018-34908-4
PubMed: 30405153
PubMed Central: PMC6220292
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Valencia</wicri:regionArea><wicri:noRegion>Valencia</wicri:noRegion></affiliation></author><author><name sortKey="Matallana, Emilia" sort="Matallana, Emilia" uniqKey="Matallana E" first="Emilia" last="Matallana">Emilia Matallana</name><affiliation wicri:level="1"><nlm:affiliation>Institute for Integrative Systems Biology, I2SysBio, University of Valencia-CSIC, Valencia, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Institute for Integrative Systems Biology, I2SysBio, University of Valencia-CSIC, Valencia</wicri:regionArea><wicri:noRegion>Valencia</wicri:noRegion></affiliation></author><author><name sortKey="Aranda, Agustin" sort="Aranda, Agustin" uniqKey="Aranda A" first="Agustín" last="Aranda">Agustín Aranda</name><affiliation wicri:level="1"><nlm:affiliation>Institute for Integrative Systems Biology, I2SysBio, University of Valencia-CSIC, Valencia, Spain. agustin.aranda@csic.es.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Institute for Integrative Systems Biology, I2SysBio, University of Valencia-CSIC, Valencia</wicri:regionArea><wicri:noRegion>Valencia</wicri:noRegion></affiliation></author></analytic><series><title level="j">Scientific reports</title><idno type="eISSN">2045-2322</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acids (metabolism)</term><term>Antioxidants (metabolism)</term><term>Gene Deletion (MeSH)</term><term>Mechanistic Target of Rapamycin Complex 1 (metabolism)</term><term>Signal Transduction (MeSH)</term><term>Thioredoxin Reductase 1 (genetics)</term><term>Thioredoxin Reductase 1 (metabolism)</term><term>Yeasts (genetics)</term><term>Yeasts (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés (métabolisme)</term><term>Antioxydants (métabolisme)</term><term>Complexe-1 cible mécanistique de la rapamycine (métabolisme)</term><term>Délétion de gène (MeSH)</term><term>Levures (génétique)</term><term>Levures (métabolisme)</term><term>Thioredoxin reductase 1 (génétique)</term><term>Thioredoxin reductase 1 (métabolisme)</term><term>Transduction du signal (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Thioredoxin Reductase 1</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Amino Acids</term><term>Antioxidants</term><term>Mechanistic Target of Rapamycin Complex 1</term><term>Thioredoxin Reductase 1</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Yeasts</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Levures</term><term>Thioredoxin reductase 1</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Yeasts</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides aminés</term><term>Antioxydants</term><term>Complexe-1 cible mécanistique de la rapamycine</term><term>Levures</term><term>Thioredoxin reductase 1</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Gene Deletion</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Délétion de gène</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The thioredoxin system plays a predominant role in the control of cellular redox status. Thioredoxin reductase fuels the system with reducing power in the form of NADPH. The TORC1 complex promotes growth and protein synthesis when nutrients, particularly amino acids, are abundant. It also represses catabolic processes, like autophagy, which are activated during starvation. We analyzed the impact of yeast cytosolic thioredoxin reductase TRR1 deletion under different environmental conditions. It shortens chronological life span and reduces growth in grape juice fermentation. TRR1 deletion has a global impact on metabolism during fermentation. As expected, it reduces oxidative stress tolerance, but a compensatory response is triggered, with catalase and glutathione increasing. Unexpectedly, TRR1 deletion causes sensitivity to the inhibitors of the TORC1 pathway, such as rapamycin. This correlates with low Tor2p kinase levels and indicates a direct role of Trr1p in its stability. Markers of TORC1 activity, however, suggest increased TORC1 activity. The autophagy caused by nitrogen starvation is reduced in the trr1Δ mutant. Ribosomal protein Rsp6p is dephosphorylated in the presence of rapamycin. This dephosphorylation diminishes in the TRR1 deletion strain. These results show a complex network of interactions between thioredoxin reductase Trr1p and the processes controlled by TOR.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30405153</PMID><DateCompleted><Year>2019</Year><Month>10</Month><Day>25</Day></DateCompleted><DateRevised><Year>2019</Year><Month>11</Month><Day>07</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2045-2322</ISSN><JournalIssue CitedMedium="Internet"><Volume>8</Volume><Issue>1</Issue><PubDate><Year>2018</Year><Month>11</Month><Day>07</Day></PubDate></JournalIssue><Title>Scientific reports</Title><ISOAbbreviation>Sci Rep</ISOAbbreviation></Journal><ArticleTitle>Yeast thioredoxin reductase Trr1p controls TORC1-regulated processes.</ArticleTitle><Pagination><MedlinePgn>16500</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/s41598-018-34908-4</ELocationID><Abstract><AbstractText>The thioredoxin system plays a predominant role in the control of cellular redox status. Thioredoxin reductase fuels the system with reducing power in the form of NADPH. The TORC1 complex promotes growth and protein synthesis when nutrients, particularly amino acids, are abundant. It also represses catabolic processes, like autophagy, which are activated during starvation. We analyzed the impact of yeast cytosolic thioredoxin reductase TRR1 deletion under different environmental conditions. It shortens chronological life span and reduces growth in grape juice fermentation. TRR1 deletion has a global impact on metabolism during fermentation. As expected, it reduces oxidative stress tolerance, but a compensatory response is triggered, with catalase and glutathione increasing. Unexpectedly, TRR1 deletion causes sensitivity to the inhibitors of the TORC1 pathway, such as rapamycin. This correlates with low Tor2p kinase levels and indicates a direct role of Trr1p in its stability. Markers of TORC1 activity, however, suggest increased TORC1 activity. The autophagy caused by nitrogen starvation is reduced in the trr1Δ mutant. Ribosomal protein Rsp6p is dephosphorylated in the presence of rapamycin. This dephosphorylation diminishes in the TRR1 deletion strain. These results show a complex network of interactions between thioredoxin reductase Trr1p and the processes controlled by TOR.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Picazo</LastName><ForeName>Cecilia</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Institute for Integrative Systems Biology, I2SysBio, University of Valencia-CSIC, Valencia, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Matallana</LastName><ForeName>Emilia</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Institute for Integrative Systems Biology, I2SysBio, University of Valencia-CSIC, Valencia, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Aranda</LastName><ForeName>Agustín</ForeName><Initials>A</Initials><Identifier Source="ORCID">http://orcid.org/0000-0003-3320-7326</Identifier><AffiliationInfo><Affiliation>Institute for Integrative Systems Biology, I2SysBio, University of Valencia-CSIC, Valencia, Spain. agustin.aranda@csic.es.</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>11</Month><Day>07</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Sci Rep</MedlineTA><NlmUniqueID>101563288</NlmUniqueID><ISSNLinking>2045-2322</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000596">Amino Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000975">Antioxidants</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.9</RegistryNumber><NameOfSubstance UI="D054481">Thioredoxin Reductase 1</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 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Agustin" sort="Aranda, Agustin" uniqKey="Aranda A" first="Agustín" last="Aranda">Agustín Aranda</name><name sortKey="Matallana, Emilia" sort="Matallana, Emilia" uniqKey="Matallana E" first="Emilia" last="Matallana">Emilia Matallana</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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