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

Content Provider	Springer Nature Link
Author	Lim, Jae Kyu Jung, Hae Chang Kang, Sung Gyun Lee, Hyun Sook
Copyright Year	2017
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.
Starting Page	491
Ending Page	498
Page Count	8
File Format	PDF
ISSN	14310651
Journal	Extremophiles
Volume Number	21
Issue Number	3
e-ISSN	14334909
Language	English
Publisher	Springer Japan
Publisher Date	2017-03-01
Publisher Place	Tokyo
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Protein disulfide oxidoreductase Thioredoxin reductase SurR Thermococcus onnurineus NA1 Redox system Microbiology Biotechnology Biochemistry Microbial Ecology
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Medicine Microbiology

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