Glutaredoxins Grx4 and Grx3 of Saccharomyces cerevisiae play a role in actin dynamics through their Trx domains, which contributes to oxidative stress resistance.
Identifieur interne : 000A24 ( Main/Exploration ); précédent : 000A23; suivant : 000A25Glutaredoxins Grx4 and Grx3 of Saccharomyces cerevisiae play a role in actin dynamics through their Trx domains, which contributes to oxidative stress resistance.
Auteurs : Nuria Pujol-Carrion [Espagne] ; Maria Angeles De La Torre-RuizSource :
- Applied and environmental microbiology [ 1098-5336 ] ; 2010.
Descripteurs français
- KwdFr :
- Actines (métabolisme), Cytosquelette (métabolisme), Espèces réactives de l'oxygène (toxicité), Glutarédoxines (métabolisme), Oxidoreductases (métabolisme), Protéines de Saccharomyces cerevisiae (métabolisme), Saccharomyces cerevisiae (enzymologie), Saccharomyces cerevisiae (physiologie), Stress oxydatif (MeSH), Structure tertiaire des protéines (MeSH), Viabilité microbienne (effets des médicaments et des substances chimiques).
- MESH :
- effets des médicaments et des substances chimiques : Viabilité microbienne.
- enzymologie : Saccharomyces cerevisiae.
- métabolisme : Actines, Cytosquelette, Glutarédoxines, Oxidoreductases, Protéines de Saccharomyces cerevisiae.
- physiologie : Saccharomyces cerevisiae.
- toxicité : Espèces réactives de l'oxygène.
- Stress oxydatif, Structure tertiaire des protéines.
English descriptors
- KwdEn :
- Actins (metabolism), Cytoskeleton (metabolism), Glutaredoxins (metabolism), Microbial Viability (drug effects), Oxidative Stress (MeSH), Oxidoreductases (metabolism), Protein Structure, Tertiary (MeSH), Reactive Oxygen Species (toxicity), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (physiology), Saccharomyces cerevisiae Proteins (metabolism).
- MESH :
- chemical , metabolism : Actins, Glutaredoxins, Oxidoreductases, Saccharomyces cerevisiae Proteins.
- drug effects : Microbial Viability.
- enzymology : Saccharomyces cerevisiae.
- metabolism : Cytoskeleton.
- physiology : Saccharomyces cerevisiae.
- chemical , toxicity : Reactive Oxygen Species.
- Oxidative Stress, Protein Structure, Tertiary.
Abstract
Grx3 and Grx4 are two monothiol glutaredoxins of Saccharomyces cerevisiae that have previously been characterized as regulators of Aft1 localization and therefore of iron homeostasis. In this study, we present data showing that both Grx3 and Grx4 have new roles in actin cytoskeleton remodeling and in cellular defenses against oxidative stress caused by reactive oxygen species (ROS) accumulation. The Grx4 protein plays a unique role in the maintenance of actin cable integrity, which is independent of its role in the transcriptional regulation of Aft1. Grx3 plays an additive and redundant role, in combination with Grx4, in the organization of the actin cytoskeleton, both under normal conditions and in response to external oxidative stress. Each Grx3 and Grx4 protein contains a thioredoxin domain sequence (Trx), followed by a glutaredoxin domain (Grx). We performed functional analyses of each of the two domains and characterized different functions for them. Each of the two Grx domains plays a role in ROS detoxification and cell viability. However, the Trx domain of each Grx4 and Grx3 protein acts independently of its respective Grx domain in a novel function that involves the polarization of the actin cytoskeleton, which also determines cell resistance against oxidative conditions. Finally, we present experimental evidence demonstrating that Grx4 behaves as an antioxidant protein increasing cell survival under conditions of oxidative stress.
DOI: 10.1128/AEM.01755-10
PubMed: 20889785
PubMed Central: PMC2988586
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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(enzymologie)</term><term>Saccharomyces cerevisiae (physiologie)</term><term>Stress oxydatif (MeSH)</term><term>Structure tertiaire des protéines (MeSH)</term><term>Viabilité microbienne (effets des médicaments et des substances chimiques)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Actins</term><term>Glutaredoxins</term><term>Oxidoreductases</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Microbial Viability</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Viabilité microbienne</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="metabolism" 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protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Grx3 and Grx4 are two monothiol glutaredoxins of Saccharomyces cerevisiae that have previously been characterized as regulators of Aft1 localization and therefore of iron homeostasis. In this study, we present data showing that both Grx3 and Grx4 have new roles in actin cytoskeleton remodeling and in cellular defenses against oxidative stress caused by reactive oxygen species (ROS) accumulation. The Grx4 protein plays a unique role in the maintenance of actin cable integrity, which is independent of its role in the transcriptional regulation of Aft1. Grx3 plays an additive and redundant role, in combination with Grx4, in the organization of the actin cytoskeleton, both under normal conditions and in response to external oxidative stress. Each Grx3 and Grx4 protein contains a thioredoxin domain sequence (Trx), followed by a glutaredoxin domain (Grx). We performed functional analyses of each of the two domains and characterized different functions for them. Each of the two Grx domains plays a role in ROS detoxification and cell viability. However, the Trx domain of each Grx4 and Grx3 protein acts independently of its respective Grx domain in a novel function that involves the polarization of the actin cytoskeleton, which also determines cell resistance against oxidative conditions. Finally, we present experimental evidence demonstrating that Grx4 behaves as an antioxidant protein increasing cell survival under conditions of oxidative stress.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20889785</PMID><DateCompleted><Year>2011</Year><Month>02</Month><Day>25</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-5336</ISSN><JournalIssue CitedMedium="Internet"><Volume>76</Volume><Issue>23</Issue><PubDate><Year>2010</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Applied and environmental microbiology</Title><ISOAbbreviation>Appl Environ Microbiol</ISOAbbreviation></Journal><ArticleTitle>Glutaredoxins Grx4 and Grx3 of Saccharomyces cerevisiae play a role in actin dynamics through their Trx domains, which contributes to oxidative stress resistance.</ArticleTitle><Pagination><MedlinePgn>7826-35</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1128/AEM.01755-10</ELocationID><Abstract><AbstractText>Grx3 and Grx4 are two monothiol glutaredoxins of Saccharomyces cerevisiae that have previously been characterized as regulators of Aft1 localization and therefore of iron homeostasis. In this study, we present data showing that both Grx3 and Grx4 have new roles in actin cytoskeleton remodeling and in cellular defenses against oxidative stress caused by reactive oxygen species (ROS) accumulation. The Grx4 protein plays a unique role in the maintenance of actin cable integrity, which is independent of its role in the transcriptional regulation of Aft1. Grx3 plays an additive and redundant role, in combination with Grx4, in the organization of the actin cytoskeleton, both under normal conditions and in response to external oxidative stress. Each Grx3 and Grx4 protein contains a thioredoxin domain sequence (Trx), followed by a glutaredoxin domain (Grx). We performed functional analyses of each of the two domains and characterized different functions for them. Each of the two Grx domains plays a role in ROS detoxification and cell viability. However, the Trx domain of each Grx4 and Grx3 protein acts independently of its respective Grx domain in a novel function that involves the polarization of the actin cytoskeleton, which also determines cell resistance against oxidative conditions. Finally, we present experimental evidence demonstrating that Grx4 behaves as an antioxidant protein increasing cell survival under conditions of oxidative stress.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Pujol-Carrion</LastName><ForeName>Nuria</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Departamento de Ciencias Médicas Básicas-IRBLleida, Facultad de Medicina, Universidad de Lleida, C/Montserrat Roig no. 2, 25008 Lleida, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>de la Torre-Ruiz</LastName><ForeName>Maria Angeles</ForeName><Initials>MA</Initials></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 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HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:20889785" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |