Salmonella Typhimurium methionine sulfoxide reductase A (MsrA) prefers TrxA in repairing methionine sulfoxide
| Autor: | Tapas Kumar Goswami, Sunil Kumar Dixit, Parvathy Rajan, Manish Mahawar, Durga Prasad Hota, Prasanta Kumar K Mishra |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Salmonella typhimurium Salmonella Thioredoxin reductase 030106 microbiology Oxidative phosphorylation Biology medicine.disease_cause Biochemistry Polymerase Chain Reaction law.invention 03 medical and health sciences chemistry.chemical_compound Methionine Thioredoxins law medicine Cloning Molecular Electrophoresis Agar Gel Methionine sulfoxide General Medicine Molecular biology Recombinant Proteins 030104 developmental biology chemistry Methionine Sulfoxide Reductases Recombinant DNA Methionine sulfoxide reductase Thioredoxin Biotechnology MSRA |
| Zdroj: | Preparative biochemistrybiotechnology. 47(2) |
| ISSN: | 1532-2297 |
| Popis: | Intraphagocytic survival of Salmonella Typhimurium (ST) depends (at least in part) upon its ability to repair oxidant-damaged macromolecules. Met residues either free or in protein bound form are highly susceptible to phagocyte-generated oxidants. Oxidation of Mets leads to Met-SO formation, consequently loss of protein functions that results in cell death. Methionine sulfoxide reductase (Msr) reductively repairs Met-SO to Met in the presence of thioredoxin (trx) and thioredoxin reductase (trxR). Earlier we reported that methionine sulfoxide reductase A (msrA) gene deletion strain of ST suffered oxidative stress.[1] Thioredoxin system of ST comprises of two thioredoxins (trxA and trxC) and one thioredoxin reductase (trxB). Preferred trx utilized in MsrA-mediated repair of Met-SO is not known. In current study, we cloned, expressed, and purified ST TrxA, TrxB, TrxC, and MsrA in recombinant forms. The migration of TrxA, TrxB, TrxC, and MsrA proteins was approximately 10, 36, 16, and 26 kDa on SDS-ge... |
| Databáze: | OpenAIRE |
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