Functional switching of ascorbate peroxidase 2 of rice (OsAPX2) between peroxidase and molecular chaperone
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چکیده
منابع مشابه
An additional cysteine in a typical 2-Cys peroxiredoxin of Pseudomonas promotes functional switching between peroxidase and molecular chaperone.
Peroxiredoxins (Prx) have received considerable attention during recent years. This study demonstrates that two typical Pseudomonas-derived 2-Cys Prx proteins, PpPrx and PaPrx can alternatively function as a peroxidase and chaperone. The amino acid sequences of these two Prx proteins exhibit 93% homology, but PpPrx possesses an additional cysteine residue, Cys112, instead of the alanine found i...
متن کاملRegulation and function of ascorbate peroxidase isoenzymes.
Even under optimal conditions, many metabolic processes, including the chloroplastic, mitochondrial, and plasma membrane-linked electron transport systems of higher plants, produce active oxygen species (AOS). Furthermore, the imposition of biotic and abiotic stress conditions can give rise to excess concentrations of AOS, resulting in oxidative damage at the cellular level. Therefore, antioxid...
متن کاملGene Knockout Study Reveals That Cytosolic Ascorbate Peroxidase 2(OsAPX2) Plays a Critical Role in Growth and Reproduction in Rice under Drought, Salt and Cold Stresses
Plant ascorbate peroxidases (APXs), enzymes catalyzing the dismutation of H2O2 into H2O and O2, play an important role in reactive oxygen species homeostasis in plants. The rice genome has eight OsAPXs, but their physiological functions remain to be determined. In this report, we studied the function of OsAPX2 gene using a T-DNA knockout mutant under the treatment of drought, salt and cold stre...
متن کاملEngineering the active site of ascorbate peroxidase.
The oxidation of a number of thioethers, namely methyl phenyl sulphide (1), ethyl phenyl sulphide (2), isopropyl phenyl sulphide (3), n-propyl phenyl sulphide (4), p-chlorophenyl methyl sulphide (5), p-nitrophenyl methyl sulphide (6) and methyl naphthalene sulphide (7), by recombinant pea cytosolic ascorbate peroxidase (rAPX) and a site-directed variant of rAPX in which the distal tryptophan 41...
متن کاملAscorbate peroxidase from soybean root nodules.
AP is involved in the destruction of harmful H202. In soybean (Glycine m a x [LI Merr.) root nodules, AP initiates a sequence of coupled redox reactions (ascorbate-GSH pathway) that results in peroxide scavenging (Dalton et al., 1986). The ascorbate-GSH pathway occurs in other plant tissues and has been extensively studied in chloroplasts where photoreducing conditions lead to the production of...
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ژورنال
عنوان ژورنال: Scientific Reports
سال: 2018
ISSN: 2045-2322
DOI: 10.1038/s41598-018-27459-1