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

Authors :
Sung Gyun Kang
Jae Kyu Lim
Hae-Chang Jung
Hyun Sook Lee
Source :
Extremophiles. 21:491-498
Publication Year :
2017
Publisher :
Springer Science and Business Media LLC, 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.

Details

ISSN :
14334909 and 14310651
Volume :
21
Database :
OpenAIRE
Journal :
Extremophiles
Accession number :
edsair.doi.dedup.....4ffbf657975cefb65943b531a65e003e
Full Text :
https://doi.org/10.1007/s00792-017-0919-1