Prokaryotic and eukaryotic monothiol glutaredoxins are able to perform the functions of Grx5 in the biogenesis of Fe/S clusters in yeast mitochondria.
Identifieur interne : 000D25 ( Main/Exploration ); précédent : 000D24; suivant : 000D26Prokaryotic and eukaryotic monothiol glutaredoxins are able to perform the functions of Grx5 in the biogenesis of Fe/S clusters in yeast mitochondria.
Auteurs : Maria Micaela Molina-Navarro [Espagne] ; Celia Casas ; Lidia Piedrafita ; Gemma Bellí ; Enrique HerreroSource :
- FEBS letters [ 0014-5793 ] ; 2006.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Embryon de poulet (cytologie), Embryon de poulet (enzymologie), Escherichia coli (enzymologie), Escherichia coli (génétique), Expression des gènes (génétique), Glutarédoxines (MeSH), Mitochondries (enzymologie), Mitochondries (génétique), Mutation (MeSH), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Poulets (génétique), Poulets (métabolisme), Protéines bactériennes (génétique), Protéines bactériennes (métabolisme), Régulation de l'expression des gènes au cours du développement (physiologie), Saccharomyces cerevisiae (enzymologie), Saccharomyces cerevisiae (génétique), Spécificité d'organe (physiologie), Synechocystis (enzymologie), Synechocystis (génétique), Évolution moléculaire (MeSH).
- MESH :
- cytologie : Embryon de poulet.
- enzymologie : Embryon de poulet, Escherichia coli, Mitochondries, Saccharomyces cerevisiae, Synechocystis.
- génétique : Escherichia coli, Expression des gènes, Mitochondries, Oxidoreductases, Poulets, Protéines bactériennes, Saccharomyces cerevisiae, Synechocystis.
- métabolisme : Oxidoreductases, Poulets, Protéines bactériennes.
- physiologie : Régulation de l'expression des gènes au cours du développement, Spécificité d'organe.
- Animaux, Glutarédoxines, Mutation, Évolution moléculaire.
English descriptors
- KwdEn :
- Animals (MeSH), Bacterial Proteins (genetics), Bacterial Proteins (metabolism), Chick Embryo (cytology), Chick Embryo (enzymology), Chickens (genetics), Chickens (metabolism), Escherichia coli (enzymology), Escherichia coli (genetics), Evolution, Molecular (MeSH), Gene Expression (genetics), Gene Expression Regulation, Developmental (physiology), Glutaredoxins (MeSH), Mitochondria (enzymology), Mitochondria (genetics), Mutation (MeSH), Organ Specificity (physiology), Oxidoreductases (genetics), Oxidoreductases (metabolism), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (genetics), Synechocystis (enzymology), Synechocystis (genetics).
- MESH :
- chemical , genetics : Bacterial Proteins, Oxidoreductases.
- chemical , metabolism : Bacterial Proteins, Oxidoreductases.
- cytology : Chick Embryo.
- enzymology : Chick Embryo, Escherichia coli, Mitochondria, Saccharomyces cerevisiae, Synechocystis.
- genetics : Chickens, Escherichia coli, Gene Expression, Mitochondria, Saccharomyces cerevisiae, Synechocystis.
- metabolism : Chickens.
- physiology : Gene Expression Regulation, Developmental, Organ Specificity.
- Animals, Evolution, Molecular, Glutaredoxins, Mutation.
Abstract
The Saccharomyces cerevisiae monothiol glutaredoxin Grx5 participates in the mitochondrial biogenesis of iron-sulfur clusters. Grx5 homologues exist in organisms from bacteria to humans. Chicken (cGRX5) and human (hGRX5) homologues contain a mitochondrial targeting sequence, suggesting a mitochondrial localization for these two proteins. We have compartmentalized the Escherichia coli and Synechocystis sp. homologues, and also cGRX5 and hGRX5, in the mitochondrial matrix of a yeast grx5 mutant. All four heterologous proteins rescue the defects of the mutant. The chicken cGRX5 gene was significantly expressed throughout the embryo stages in different tissues. These results underline the functional conservation of Grx5 homologues throughout evolution.
DOI: 10.1016/j.febslet.2006.03.037
PubMed: 16566929
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Molecular</term><term>Glutaredoxins</term><term>Mutation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Glutarédoxines</term><term>Mutation</term><term>Évolution moléculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The Saccharomyces cerevisiae monothiol glutaredoxin Grx5 participates in the mitochondrial biogenesis of iron-sulfur clusters. Grx5 homologues exist in organisms from bacteria to humans. Chicken (cGRX5) and human (hGRX5) homologues contain a mitochondrial targeting sequence, suggesting a mitochondrial localization for these two proteins. We have compartmentalized the Escherichia coli and Synechocystis sp. homologues, and also cGRX5 and hGRX5, in the mitochondrial matrix of a yeast grx5 mutant. All four heterologous proteins rescue the defects of the mutant. The chicken cGRX5 gene was significantly expressed throughout the embryo stages in different tissues. These results underline the functional conservation of Grx5 homologues throughout evolution.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16566929</PMID><DateCompleted><Year>2006</Year><Month>06</Month><Day>05</Day></DateCompleted><DateRevised><Year>2007</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0014-5793</ISSN><JournalIssue CitedMedium="Print"><Volume>580</Volume><Issue>9</Issue><PubDate><Year>2006</Year><Month>Apr</Month><Day>17</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Prokaryotic and eukaryotic monothiol glutaredoxins are able to perform the functions of Grx5 in the biogenesis of Fe/S clusters in yeast mitochondria.</ArticleTitle><Pagination><MedlinePgn>2273-80</MedlinePgn></Pagination><Abstract><AbstractText>The Saccharomyces cerevisiae monothiol glutaredoxin Grx5 participates in the mitochondrial biogenesis of iron-sulfur clusters. Grx5 homologues exist in organisms from bacteria to humans. Chicken (cGRX5) and human (hGRX5) homologues contain a mitochondrial targeting sequence, suggesting a mitochondrial localization for these two proteins. We have compartmentalized the Escherichia coli and Synechocystis sp. homologues, and also cGRX5 and hGRX5, in the mitochondrial matrix of a yeast grx5 mutant. All four heterologous proteins rescue the defects of the mutant. The chicken cGRX5 gene was significantly expressed throughout the embryo stages in different tissues. These results underline the functional conservation of Grx5 homologues throughout evolution.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Molina-Navarro</LastName><ForeName>Maria Micaela</ForeName><Initials>MM</Initials><AffiliationInfo><Affiliation>Departament de Ciències Mèdiques Bàsiques, Facultat de Medicina, Universitat de Lleida, Montserrat Roig 2, 25008-Lleida, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Casas</LastName><ForeName>Celia</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Piedrafita</LastName><ForeName>Lidia</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Bellí</LastName><ForeName>Gemma</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Herrero</LastName><ForeName>Enrique</ForeName><Initials>E</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative 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