Characterization of a multifunctional protein disulfide oxidoreductase from Sulfolobus solfataricus(424 views) Pedone E, Limauro D, D'Alterio R, Rossi M, Bartolucci S
Keywords: Protein Disulfide Oxidoreductases (pdo), Redox Sites, Sulfolobus Solfataricus, Thermophiles, Thioredoxin System, Bacterial Protein, Cell Protein, Chaperone, Isomerase, Thioredoxin Reductase, Aerobic Bacteria, Article, Controlled Study, Cytoplasm, Disulfide Bond, Enzyme Activity, Enzyme Substrate, Escherichia Coli, Nonhuman, Northern Blotting, Oxidation Reduction Reaction, Oxidative Stress, Priority Journal, Protein Analysis, Protein Expression, Protein Folding, Protein Isolation, Thermophilic Bacterium, Western Blotting, Amino Acid Sequence, Cysteine, Fluorescent Dyes, Molecular Chaperones, Molecular Sequence Data, Protein Disulfide Reductase (glutathione), Sequence Alignment, Time Factors, Archaea,
Affiliations: *** IBB - CNR ***
Dipartimento di Biologia Strutturale e Funzionale, Complesso Universitario di Monte S. Angelo, Università di Napoli 'Federico II', Via Cinthia, 80126 Naples, Italy
Istituto di Biostrutture e Bioimmagini, C.N.R., Naples, Italy
Istituto di Biochimica Delle Proteine, C.N.R., Naples, Italy
References: Not available.
Characterization of a multifunctional protein disulfide oxidoreductase from Sulfolobus solfataricus
A potential role in disulfide bond formation in the intracellular proteins of thermophilic organisms has recently been ascribed to a new family of protein disulfide oxidoreductases (PDOs). We report on the characterization of SsPDO, isolated from the hyperthermophilic archaeon Sulfolobus solfataricus. SsPDO was cloned and expressed in Escherichia coli. We revealed that SsPDO is the substrate of a thioredoxin reductase in S. solfataricus (K-M 0.3 mu M) and not thioredoxins (TrxA1 and TrxA2). SsPDO/S. solfataricus thioredoxin reductase constitute a new thioredoxin system in aerobic thermophilic archaea. While redox (reductase, oxidative and isomerase) activities of SsPDO point to its central role in the biochemistry of cytoplasmic disulfide bonds, chaperone activities also on an endogenous substrate suggest a potential role in the stabilization of intracellular proteins. Northern and western analysis have been performed in order to analyze the response to the oxidative stress.
Characterization of a multifunctional protein disulfide oxidoreductase from Sulfolobus solfataricus
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Characterization of a multifunctional protein disulfide oxidoreductase from Sulfolobus solfataricus