GlutaredoxinV1, Main, Exploration, bibRecord, 001080

A viral member of the ERV1/ALR protein family participates in a cytoplasmic pathway of disulfide bond formation.

Identifieur interne : 001080 ( Main/Exploration ); précédent : 001079; suivant : 001081

A viral member of the ERV1/ALR protein family participates in a cytoplasmic pathway of disulfide bond formation.

Auteurs : T G Senkevich [États-Unis] ; C L White ; E V Koonin ; B. Moss

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2000.

RBID : pubmed:11035794

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Cysteine (metabolism), DNA-Binding Proteins (chemistry), DNA-Binding Proteins (metabolism), Disulfides (metabolism), Fungal Proteins (chemistry), Fungal Proteins (metabolism), Mitochondrial Proteins (MeSH), Molecular Sequence Data (MeSH), Neoplasm Proteins (MeSH), Open Reading Frames (MeSH), Oxidoreductases Acting on Sulfur Group Donors (MeSH), Saccharomyces cerevisiae Proteins (MeSH), Sequence Homology, Amino Acid (MeSH), Vaccinia virus (metabolism).
MESH :
- chemical , chemistry : DNA-Binding Proteins, Fungal Proteins.
- chemical , metabolism : Cysteine, DNA-Binding Proteins, Disulfides, Fungal Proteins.
- metabolism : Vaccinia virus.
- Amino Acid Sequence, Mitochondrial Proteins, Molecular Sequence Data, Neoplasm Proteins, Open Reading Frames, Oxidoreductases Acting on Sulfur Group Donors, Saccharomyces cerevisiae Proteins, Sequence Homology, Amino Acid.

Abstract

Proteins of the ERV1/ALR family are encoded by all eukaryotes and cytoplasmic DNA viruses for which substantial sequence information is available. Nevertheless, the roles of these proteins are imprecisely known. Multiple alignments of ERV1/ALR proteins indicated an invariant C-X-X-C motif, but no similarity to the thioredoxin fold was revealed by secondary structure predictions. We chose a virus model to investigate the role of these proteins as thiol oxidoreductases. When cells were infected with a mutant vaccinia virus in which the E10R gene encoding an ERV1/ALR family protein was repressed, the disulfide bonds of three other viral proteins-namely, the L1R and F9L proteins and the G4L glutaredoxin-were completely reduced. The same outcome occurred when Cys-43 or Cys-46, the putative redox cysteines of the E10R protein, was mutated to serine. These two cysteines were disulfide bonded during a normal virus infection but not if the synthesis of other viral late proteins was inhibited or the E10R protein was expressed by itself in uninfected cells, suggesting a requirement for an upstream viral thiol oxidoreductase. Remarkably, the cysteine-containing domains of the E10R and L1R viral membrane proteins and the glutaredoxin are in the cytoplasm, in which assembly of vaccinia virions occurs, rather than in the oxidizing environment of the endoplasmic reticulum. These data indicated a viral pathway of disulfide bond formation in which the E10R protein has a central role. By extension, the ERV1/ALR family may represent a ubiquitous class of cellular thiol oxidoreductases that interact with glutaredoxins or thioredoxins.

DOI: 10.1073/pnas.210397997
PubMed: 11035794
PubMed Central: PMC17295

Affiliations:

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

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Le document en format XML

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<term>Neoplasm Proteins (MeSH)</term>
<term>Open Reading Frames (MeSH)</term>
<term>Oxidoreductases Acting on Sulfur Group Donors (MeSH)</term>
<term>Saccharomyces cerevisiae Proteins (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Cadres ouverts de lecture (MeSH)</term>
<term>Cystéine (métabolisme)</term>
<term>Disulfures (métabolisme)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Oxidoreductases acting on sulfur group donors (MeSH)</term>
<term>Protéines de Saccharomyces cerevisiae (MeSH)</term>
<term>Protéines de liaison à l'ADN (composition chimique)</term>
<term>Protéines de liaison à l'ADN (métabolisme)</term>
<term>Protéines fongiques (composition chimique)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Protéines mitochondriales (MeSH)</term>
<term>Protéines tumorales (MeSH)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Virus de la vaccine (métabolisme)</term>
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<term>Fungal Proteins</term>
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<term>Protéines de liaison à l'ADN</term>
<term>Protéines fongiques</term>
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<term>Open Reading Frames</term>
<term>Oxidoreductases Acting on Sulfur Group Donors</term>
<term>Saccharomyces cerevisiae Proteins</term>
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<term>Protéines mitochondriales</term>
<term>Protéines tumorales</term>
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<front><div type="abstract" xml:lang="en">Proteins of the ERV1/ALR family are encoded by all eukaryotes and cytoplasmic DNA viruses for which substantial sequence information is available. Nevertheless, the roles of these proteins are imprecisely known. Multiple alignments of ERV1/ALR proteins indicated an invariant C-X-X-C motif, but no similarity to the thioredoxin fold was revealed by secondary structure predictions. We chose a virus model to investigate the role of these proteins as thiol oxidoreductases. When cells were infected with a mutant vaccinia virus in which the E10R gene encoding an ERV1/ALR family protein was repressed, the disulfide bonds of three other viral proteins-namely, the L1R and F9L proteins and the G4L glutaredoxin-were completely reduced. The same outcome occurred when Cys-43 or Cys-46, the putative redox cysteines of the E10R protein, was mutated to serine. These two cysteines were disulfide bonded during a normal virus infection but not if the synthesis of other viral late proteins was inhibited or the E10R protein was expressed by itself in uninfected cells, suggesting a requirement for an upstream viral thiol oxidoreductase. Remarkably, the cysteine-containing domains of the E10R and L1R viral membrane proteins and the glutaredoxin are in the cytoplasm, in which assembly of vaccinia virions occurs, rather than in the oxidizing environment of the endoplasmic reticulum. These data indicated a viral pathway of disulfide bond formation in which the E10R protein has a central role. By extension, the ERV1/ALR family may represent a ubiquitous class of cellular thiol oxidoreductases that interact with glutaredoxins or thioredoxins.</div>
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<name sortKey="Moss, B" sort="Moss, B" uniqKey="Moss B" first="B" last="Moss">B. Moss</name>
<name sortKey="White, C L" sort="White, C L" uniqKey="White C" first="C L" last="White">C L White</name>
</noCountry>
<country name="États-Unis"><region name="Maryland"><name sortKey="Senkevich, T G" sort="Senkevich, T G" uniqKey="Senkevich T" first="T G" last="Senkevich">T G Senkevich</name>
</region>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Bois/explor/GlutaredoxinV1/Data/Main/Exploration

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001080 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 001080 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Bois
   |area=    GlutaredoxinV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:11035794
   |texte=   A viral member of the ERV1/ALR protein family participates in a cytoplasmic pathway of disulfide bond formation.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:11035794" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a GlutaredoxinV1

This area was generated with Dilib version V0.6.37.
Data generation: Wed Nov 18 15:13:42 2020. Site generation: Wed Nov 18 15:16:12 2020

	Serveur d'exploration sur la glutarédoxine
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration sur la glutarédoxine

A viral member of the ERV1/ALR protein family participates in a cytoplasmic pathway of disulfide bond formation.

A viral member of the ERV1/ALR protein family participates in a cytoplasmic pathway of disulfide bond formation.

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Abstract

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

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki