GlutaredoxinV1, Main, Exploration, bibRecord, 001287

Glutaredoxin homolog encoded by vaccinia virus is a virion-associated enzyme with thioltransferase and dehydroascorbate reductase activities.

Identifieur interne : 001287 ( Main/Exploration ); précédent : 001286; suivant : 001288

Glutaredoxin homolog encoded by vaccinia virus is a virion-associated enzyme with thioltransferase and dehydroascorbate reductase activities.

Auteurs : B Y Ahn [États-Unis] ; B. Moss

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 1992.

RBID : pubmed:1496000

Descripteurs français

English descriptors

KwdEn :
- Animals (MeSH), Bacterial Proteins (genetics), Base Sequence (MeSH), Cell Line (MeSH), Chromatography, Ion Exchange (MeSH), Cloning, Molecular (MeSH), Escherichia coli (genetics), Glutaredoxins (MeSH), HeLa Cells (MeSH), Humans (MeSH), Molecular Sequence Data (MeSH), NADP Transhydrogenases (genetics), NADP Transhydrogenases (isolation & purification), NADP Transhydrogenases (metabolism), Oligodeoxyribonucleotides (MeSH), Open Reading Frames (MeSH), Oxidoreductases (genetics), Oxidoreductases (isolation & purification), Oxidoreductases (metabolism), Protein Disulfide Reductase (Glutathione) (MeSH), Proteins (genetics), Proteins (isolation & purification), Recombinant Proteins (isolation & purification), Recombinant Proteins (metabolism), Vaccinia virus (enzymology), Vaccinia virus (genetics), Viral Plaque Assay (MeSH), Virion (enzymology), Virion (genetics).
MESH :
- chemical , genetics : Bacterial Proteins, NADP Transhydrogenases, Oxidoreductases, Proteins.
- enzymology : Vaccinia virus, Virion.
- genetics : Escherichia coli, Vaccinia virus, Virion.
- chemical , isolation & purification : NADP Transhydrogenases, Oxidoreductases, Proteins, Recombinant Proteins.
- chemical , metabolism : NADP Transhydrogenases, Oxidoreductases, Recombinant Proteins.
- Animals, Base Sequence, Cell Line, Chromatography, Ion Exchange, Cloning, Molecular, Glutaredoxins, HeLa Cells, Humans, Molecular Sequence Data, Oligodeoxyribonucleotides, Open Reading Frames, Protein Disulfide Reductase (Glutathione), Viral Plaque Assay.

Abstract

Glutaredoxins (GRXs), also known as thioltransferases, use glutathione as a cofactor for reduction of disulfides in prokaryotes and eukaryotes. We demonstrate that the vaccinia virus O2L open reading frame encodes a functional GRX, as predicted by Johnson et al. [Johnson, G. P., Goebel, S. J., Perkus, M. E., Davis, S. W., Winslow, J. P. & Paoletti, E. (1991) Virology 181, 378-381] from sequence homology. The 12-kDa protein product of the O2L open reading frame was synthesized after viral DNA replication, coincident with a major increase in cytoplasmic glutathione-dependent thioltransferase activity. The protein was associated with purified vaccinia virions and was not released by treatment with a nonionic detergent unless dithiothreitol was added. The virion-derived protein, as well as a recombinant form expressed in Escherichia coli, exhibited thioltransferase and dehydroascorbate reductase activities indicative of a functional GRX. The postreplicative synthesis of vaccinia virus GRX and its association with virions suggest that the enzyme may have novel roles in the virus growth cycle.

DOI: 10.1073/pnas.89.15.7060
PubMed: 1496000
PubMed Central: PMC49645

Affiliations:

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Le document en format XML

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<term>Chromatography, Ion Exchange (MeSH)</term>
<term>Cloning, Molecular (MeSH)</term>
<term>Escherichia coli (genetics)</term>
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<term>HeLa Cells (MeSH)</term>
<term>Humans (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>NADP Transhydrogenases (genetics)</term>
<term>NADP Transhydrogenases (isolation & purification)</term>
<term>NADP Transhydrogenases (metabolism)</term>
<term>Oligodeoxyribonucleotides (MeSH)</term>
<term>Open Reading Frames (MeSH)</term>
<term>Oxidoreductases (genetics)</term>
<term>Oxidoreductases (isolation & purification)</term>
<term>Oxidoreductases (metabolism)</term>
<term>Protein Disulfide Reductase (Glutathione) (MeSH)</term>
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<term>Proteins (isolation & purification)</term>
<term>Recombinant Proteins (isolation & purification)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>Vaccinia virus (enzymology)</term>
<term>Vaccinia virus (genetics)</term>
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<term>Glutarédoxines (MeSH)</term>
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<term>Méthode des plages virales (MeSH)</term>
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<term>NADP transhydrogenases (isolement et purification)</term>
<term>NADP transhydrogenases (métabolisme)</term>
<term>Oligodésoxyribonucléotides (MeSH)</term>
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<term>Oxidoreductases (isolement et purification)</term>
<term>Oxidoreductases (métabolisme)</term>
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<term>Protéines recombinantes (isolement et purification)</term>
<term>Protéines recombinantes (métabolisme)</term>
<term>Séquence nucléotidique (MeSH)</term>
<term>Virion (enzymologie)</term>
<term>Virion (génétique)</term>
<term>Virus de la vaccine (enzymologie)</term>
<term>Virus de la vaccine (génétique)</term>
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<term>Proteins</term>
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<term>Virus de la vaccine</term>
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<term>Virion</term>
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<term>Vaccinia virus</term>
<term>Virion</term>
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<term>Oxidoreductases</term>
<term>Protéines</term>
<term>Protéines bactériennes</term>
<term>Virion</term>
<term>Virus de la vaccine</term>
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<term>Oxidoreductases</term>
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<term>Recombinant Proteins</term>
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<term>Oxidoreductases</term>
<term>Protéines</term>
<term>Protéines recombinantes</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>NADP Transhydrogenases</term>
<term>Oxidoreductases</term>
<term>Recombinant Proteins</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>NADP transhydrogenases</term>
<term>Oxidoreductases</term>
<term>Protéines recombinantes</term>
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<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Base Sequence</term>
<term>Cell Line</term>
<term>Chromatography, Ion Exchange</term>
<term>Cloning, Molecular</term>
<term>Glutaredoxins</term>
<term>HeLa Cells</term>
<term>Humans</term>
<term>Molecular Sequence Data</term>
<term>Oligodeoxyribonucleotides</term>
<term>Open Reading Frames</term>
<term>Protein Disulfide Reductase (Glutathione)</term>
<term>Viral Plaque Assay</term>
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<term>Cadres ouverts de lecture</term>
<term>Cellules HeLa</term>
<term>Chromatographie d'échange d'ions</term>
<term>Clonage moléculaire</term>
<term>Données de séquences moléculaires</term>
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<term>Humains</term>
<term>Lignée cellulaire</term>
<term>Méthode des plages virales</term>
<term>Oligodésoxyribonucléotides</term>
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<front><div type="abstract" xml:lang="en">Glutaredoxins (GRXs), also known as thioltransferases, use glutathione as a cofactor for reduction of disulfides in prokaryotes and eukaryotes. We demonstrate that the vaccinia virus O2L open reading frame encodes a functional GRX, as predicted by Johnson et al. [Johnson, G. P., Goebel, S. J., Perkus, M. E., Davis, S. W., Winslow, J. P. & Paoletti, E. (1991) Virology 181, 378-381] from sequence homology. The 12-kDa protein product of the O2L open reading frame was synthesized after viral DNA replication, coincident with a major increase in cytoplasmic glutathione-dependent thioltransferase activity. The protein was associated with purified vaccinia virions and was not released by treatment with a nonionic detergent unless dithiothreitol was added. The virion-derived protein, as well as a recombinant form expressed in Escherichia coli, exhibited thioltransferase and dehydroascorbate reductase activities indicative of a functional GRX. The postreplicative synthesis of vaccinia virus GRX and its association with virions suggest that the enzyme may have novel roles in the virus growth cycle.</div>
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<Abstract><AbstractText>Glutaredoxins (GRXs), also known as thioltransferases, use glutathione as a cofactor for reduction of disulfides in prokaryotes and eukaryotes. We demonstrate that the vaccinia virus O2L open reading frame encodes a functional GRX, as predicted by Johnson et al. [Johnson, G. P., Goebel, S. J., Perkus, M. E., Davis, S. W., Winslow, J. P. & Paoletti, E. (1991) Virology 181, 378-381] from sequence homology. The 12-kDa protein product of the O2L open reading frame was synthesized after viral DNA replication, coincident with a major increase in cytoplasmic glutathione-dependent thioltransferase activity. The protein was associated with purified vaccinia virions and was not released by treatment with a nonionic detergent unless dithiothreitol was added. The virion-derived protein, as well as a recombinant form expressed in Escherichia coli, exhibited thioltransferase and dehydroascorbate reductase activities indicative of a functional GRX. The postreplicative synthesis of vaccinia virus GRX and its association with virions suggest that the enzyme may have novel roles in the virus growth cycle.</AbstractText>
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Glutaredoxin homolog encoded by vaccinia virus is a virion-associated enzyme with thioltransferase and dehydroascorbate reductase activities.

Glutaredoxin homolog encoded by vaccinia virus is a virion-associated enzyme with thioltransferase and dehydroascorbate reductase activities.

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