Redox regulation of SurR by protein disulfide oxidoreductase in Thermococcus onnurineus NA1
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Title
- Redox regulation of SurR by protein disulfide oxidoreductase in Thermococcus onnurineus NA1
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Author(s)
- Lim, Jae Kyu; Jung, Hae-Chang; Kang, Sung Gyun; Lee, Hyun Sook
- KIOST Author(s)
- Lim, Jae Kyu(임재규); Kang, Sung Gyun(강성균); Lee, Hyun Sook(이현숙)
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Alternative Author(s)
- 임재규; 정해창; 강성균; 이현숙
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Publication Year
- 2017-05
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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.
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ISSN
- 1431-0651
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URI
- https://sciwatch.kiost.ac.kr/handle/2020.kiost/1246
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DOI
- 10.1007/s00792-017-0919-1
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Bibliographic Citation
- EXTREMOPHILES, v.21, no.3, pp.491 - 498, 2017
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Publisher
- SPRINGER JAPAN KK
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Keywords
- Protein disulfide oxidoreductase; Thioredoxin reductase; SurR; Thermococcus onnurineus NA1; Redox system
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Type
- Article
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Language
- English
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Document Type
- Article
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