GlutaredoxinV1, Main, Exploration, bibRecord, 000319

Redox regulation of SurR by protein disulfide oxidoreductase in Thermococcus onnurineus NA1.

Identifieur interne : 000319 ( Main/Exploration ); précédent : 000318; suivant : 000320

Redox regulation of SurR by protein disulfide oxidoreductase in Thermococcus onnurineus NA1.

Auteurs : Jae Kyu Lim [Corée du Sud] ; Hae-Chang Jung [Corée du Sud] ; Sung Gyun Kang [Corée du Sud] ; Hyun Sook Lee [Corée du Sud]

Source :

Extremophiles : life under extreme conditions [ 1433-4909 ] ; 2017.

RBID : pubmed:28251348

Descripteurs français

KwdFr :
- Liaison aux protéines (MeSH), Oxydoréduction (MeSH), Protéines d'archée (composition chimique), Protéines d'archée (génétique), Protéines d'archée (métabolisme), Similitude de séquences (MeSH), Soufre (métabolisme), Thermococcus (enzymologie), Thermococcus (génétique), Thermococcus (métabolisme), Thioredoxin-disulfide reductase (composition chimique), Thioredoxin-disulfide reductase (génétique), Thioredoxin-disulfide reductase (métabolisme).
MESH :
- composition chimique : Protéines d'archée, Thioredoxin-disulfide reductase.
- enzymologie : Thermococcus.
- génétique : Protéines d'archée, Thermococcus, Thioredoxin-disulfide reductase.
- métabolisme : Protéines d'archée, Soufre, Thermococcus, Thioredoxin-disulfide reductase.
- Liaison aux protéines, Oxydoréduction, Similitude de séquences.

English descriptors

KwdEn :
- Archaeal Proteins (chemistry), Archaeal Proteins (genetics), Archaeal Proteins (metabolism), Oxidation-Reduction (MeSH), Protein Binding (MeSH), Sequence Homology (MeSH), Sulfur (metabolism), Thermococcus (enzymology), Thermococcus (genetics), Thermococcus (metabolism), Thioredoxin-Disulfide Reductase (chemistry), Thioredoxin-Disulfide Reductase (genetics), Thioredoxin-Disulfide Reductase (metabolism).
MESH :
- chemical , chemistry : Archaeal Proteins, Thioredoxin-Disulfide Reductase.
- chemical , genetics : Archaeal Proteins, Thioredoxin-Disulfide Reductase.
- chemical , metabolism : Archaeal Proteins, Sulfur, Thioredoxin-Disulfide Reductase.
- enzymology : Thermococcus.
- genetics : Thermococcus.
- metabolism : Thermococcus.
- Oxidation-Reduction, Protein Binding, Sequence Homology.

Abstract

Protein disulfide oxidoreductases are redox enzymes that catalyze thiol-disulfide exchange reactions. These enzymes include thioredoxins, glutaredoxins, protein disulfide isomerases, disulfide bond formation A (DsbA) proteins, and Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO) homologues. In the genome of a hyperthermophilic archaeon, Thermococcus onnurineus NA1, the genes encoding one PfPDO homologue (TON_0319, Pdo) and three more thioredoxin- or glutaredoxin-like proteins (TON_0470, TON_0472, TON_0834) were identified. All except TON_0470 were recombinantly expressed and purified. Three purified proteins were reduced by a thioredoxin reductase (TrxR), indicating that each protein can form redox complex with TrxR. SurR, a transcription factor involved in the sulfur response, was tested for a protein target of a TrxR-redoxin system and only Pdo was identified to be capable of catalyzing the reduction of SurR. Electromobility shift assay demonstrated that SurR reduced by the TrxR-Pdo system could bind to the DNA probe with the SurR-binding motif, GTTttgAAC. In this study, we present the TrxR-Pdo couple as a redox-regulator for SurR in T. onnurineus NA1.

DOI: 10.1007/s00792-017-0919-1
PubMed: 28251348

Affiliations:

Corée du Sud

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

to stream Main, to step Corpus: 000364
to stream Main, to step Curation: 000364

Le document en format XML

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<front><div type="abstract" xml:lang="en">Protein disulfide oxidoreductases are redox enzymes that catalyze thiol-disulfide exchange reactions. These enzymes include thioredoxins, glutaredoxins, protein disulfide isomerases, disulfide bond formation A (DsbA) proteins, and Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO) homologues. In the genome of a hyperthermophilic archaeon, Thermococcus onnurineus NA1, the genes encoding one PfPDO homologue (TON_0319, Pdo) and three more thioredoxin- or glutaredoxin-like proteins (TON_0470, TON_0472, TON_0834) were identified. All except TON_0470 were recombinantly expressed and purified. Three purified proteins were reduced by a thioredoxin reductase (TrxR), indicating that each protein can form redox complex with TrxR. SurR, a transcription factor involved in the sulfur response, was tested for a protein target of a TrxR-redoxin system and only Pdo was identified to be capable of catalyzing the reduction of SurR. Electromobility shift assay demonstrated that SurR reduced by the TrxR-Pdo system could bind to the DNA probe with the SurR-binding motif, GTTttgAAC. In this study, we present the TrxR-Pdo couple as a redox-regulator for SurR in T. onnurineus NA1.</div>
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<Abstract><AbstractText>Protein disulfide oxidoreductases are redox enzymes that catalyze thiol-disulfide exchange reactions. These enzymes include thioredoxins, glutaredoxins, protein disulfide isomerases, disulfide bond formation A (DsbA) proteins, and Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO) homologues. In the genome of a hyperthermophilic archaeon, Thermococcus onnurineus NA1, the genes encoding one PfPDO homologue (TON_0319, Pdo) and three more thioredoxin- or glutaredoxin-like proteins (TON_0470, TON_0472, TON_0834) were identified. All except TON_0470 were recombinantly expressed and purified. Three purified proteins were reduced by a thioredoxin reductase (TrxR), indicating that each protein can form redox complex with TrxR. SurR, a transcription factor involved in the sulfur response, was tested for a protein target of a TrxR-redoxin system and only Pdo was identified to be capable of catalyzing the reduction of SurR. Electromobility shift assay demonstrated that SurR reduced by the TrxR-Pdo system could bind to the DNA probe with the SurR-binding motif, GTTttgAAC. In this study, we present the TrxR-Pdo couple as a redox-regulator for SurR in T. onnurineus NA1.</AbstractText>
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Redox regulation of SurR by protein disulfide oxidoreductase in Thermococcus onnurineus NA1.

Redox regulation of SurR by protein disulfide oxidoreductase in Thermococcus onnurineus NA1.

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