Keywords: Glutaredoxin, Protein Disulfide Isomerase, Protein Disulfide Reductase (glutathione), Thioredoxin, Catalysis, Chimera, Disulfide Bond, Homeostasis, Human, Mesophilic Bacterium, Nonhuman, Nucleotide Sequence, Oxidation, Oxidation Reduction Reaction, Priority Journal, Protein Analysis, Protein Folding, Protein Function, Protein Structure, Review, Thermophile, Amino Acid Sequence, Models, Molecular, Molecular Sequence Data, Oxidation-Reduction, Protein Disulfide-Isomerase, Sequence Homology, Bacteria (microorganisms), Eukaryota, Prokaryota, Erratum,
Affiliations: *** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, C.N.R., Complesso Universitario Monte S. Angelo, Naples, Italy
Dip. Biologia Strutturale e Funzionale, University of Naples Federico II, Complesso Universitario Monte S. Angelo, Naples, Italy
References: Not available.
The machinery for oxidative protein folding in thermophiles
Disulfide bonds are required for the stability and function of many proteins. A large number of thiol-disulfide oxidoreductases, belonging to the thioredoxin superfamily, catalyze protein disulfide bond formation in all living cells, from bacteria to humans. The protein disulfide isomerase (PDI) is the eukaryotic factor that catalyzes oxidative protein folding in the endoplasmic reticulum; by contrast, in prokaryotes, a family of disulfide bond (Dsb) proteins have an equivalent outcome in the bacterial periplasm. Recently the results from genome analysis suggested an important role for disulfide bonds in the structural stabilization of intracellular proteins from thermophiles. A specific protein disulfide oxidoreductase (PDO) has a key role in intracellular disulfide shuffling in thermophiles. Here we focus on the structural and functional characterization of PDO correlated with the multifunctional eukaryotic PDI. In addition, we highlight the chimeric nature of the machinery for oxidative protein folding in thermophiles in comparison with the mesophilic bacterial and eukaryal counterparts.
The machinery for oxidative protein folding in thermophiles