GlutaredoxinV1, Main, Exploration, bibRecord, 000B77

Redox control and oxidative stress in yeast cells.

Identifieur interne : 000B77 ( Main/Exploration ); précédent : 000B76; suivant : 000B78

Redox control and oxidative stress in yeast cells.

Auteurs : Enrique Herrero [Espagne] ; Joaquim Ros ; Gemma Bellí ; Elisa Cabiscol

Source :

Biochimica et biophysica acta [ 0006-3002 ] ; 2008.

RBID : pubmed:18178164

Descripteurs français

KwdFr :
- Antioxydants (métabolisme), Espèces réactives de l'oxygène (métabolisme), Humains (MeSH), Oxydoréduction (MeSH), Protéines associées à la pancréatite (MeSH), Saccharomyces cerevisiae (cytologie), Saccharomyces cerevisiae (métabolisme), Stress oxydatif (MeSH).
MESH :
- cytologie : Saccharomyces cerevisiae.
- métabolisme : Antioxydants, Espèces réactives de l'oxygène, Saccharomyces cerevisiae.
- Humains, Oxydoréduction, Protéines associées à la pancréatite, Stress oxydatif.

English descriptors

KwdEn :
- Antioxidants (metabolism), Humans (MeSH), Oxidation-Reduction (MeSH), Oxidative Stress (MeSH), Pancreatitis-Associated Proteins (MeSH), Reactive Oxygen Species (metabolism), Saccharomyces cerevisiae (cytology), Saccharomyces cerevisiae (metabolism).
MESH :
- chemical , metabolism : Antioxidants, Reactive Oxygen Species.
- cytology : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Humans, Oxidation-Reduction, Oxidative Stress, Pancreatitis-Associated Proteins.

Abstract

Protein structure and function can be altered by reactive oxygen species produced either by cell metabolism or by external oxidants. Although catalases, superoxide dismutases and peroxidases contribute to maintaining non-toxic levels of reactive oxygen species, modification of amino acid side chains occurs. In particular, oxidative modification of sulphydryl groups in proteins can be a two-faceted process: it could lead to impairment of protein function or, depending on the redox state of cysteine residues, may activate specific pathways involved in regulating key cell functions. In yeast cells, the thioredoxin and glutaredoxin systems participate in such redox regulation in different cell compartments, and interplay exists between both systems. In this context, glutaredoxins with monothiol activity initially characterised in Saccharomyces cerevisiae may display specific regulatory functions at the mitochondria and nuclei. Furthermore, their structural conservation in other organisms point to a conserved important role in metal homeostasis also in higher eukaryotes. Control of gene expression in response to oxidative stress is mediated by several transcription factors, among which Yap1 has a predominant role in S. cerevisiae (Pap1 in Schizosaccharomyces pombe and Cap1 in Candida albicans). In combination with Gpx3 peroxidase and Ybp1 protein, the activity of Yap1 is itself controlled depending on the redox state of some of its cysteine residues, which determines the nucleocytoplasmic location of the Yap1 molecules.

DOI: 10.1016/j.bbagen.2007.12.004
PubMed: 18178164

Affiliations:

Espagne

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Le document en format XML

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<term>Pancreatitis-Associated Proteins (MeSH)</term>
<term>Reactive Oxygen Species (metabolism)</term>
<term>Saccharomyces cerevisiae (cytology)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Antioxydants (métabolisme)</term>
<term>Espèces réactives de l'oxygène (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Protéines associées à la pancréatite (MeSH)</term>
<term>Saccharomyces cerevisiae (cytologie)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Stress oxydatif (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antioxidants</term>
<term>Reactive Oxygen Species</term>
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<keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Antioxydants</term>
<term>Espèces réactives de l'oxygène</term>
<term>Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" xml:lang="en"><term>Humans</term>
<term>Oxidation-Reduction</term>
<term>Oxidative Stress</term>
<term>Pancreatitis-Associated Proteins</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Humains</term>
<term>Oxydoréduction</term>
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<front><div type="abstract" xml:lang="en">Protein structure and function can be altered by reactive oxygen species produced either by cell metabolism or by external oxidants. Although catalases, superoxide dismutases and peroxidases contribute to maintaining non-toxic levels of reactive oxygen species, modification of amino acid side chains occurs. In particular, oxidative modification of sulphydryl groups in proteins can be a two-faceted process: it could lead to impairment of protein function or, depending on the redox state of cysteine residues, may activate specific pathways involved in regulating key cell functions. In yeast cells, the thioredoxin and glutaredoxin systems participate in such redox regulation in different cell compartments, and interplay exists between both systems. In this context, glutaredoxins with monothiol activity initially characterised in Saccharomyces cerevisiae may display specific regulatory functions at the mitochondria and nuclei. Furthermore, their structural conservation in other organisms point to a conserved important role in metal homeostasis also in higher eukaryotes. Control of gene expression in response to oxidative stress is mediated by several transcription factors, among which Yap1 has a predominant role in S. cerevisiae (Pap1 in Schizosaccharomyces pombe and Cap1 in Candida albicans). In combination with Gpx3 peroxidase and Ybp1 protein, the activity of Yap1 is itself controlled depending on the redox state of some of its cysteine residues, which determines the nucleocytoplasmic location of the Yap1 molecules.</div>
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Redox control and oxidative stress in yeast cells.

Redox control and oxidative stress in yeast cells.

Source :

Descripteurs français

English descriptors

Abstract

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

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

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Pour générer des pages wiki