menadione/oryza sativa

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Expression of salt-induced 2-Cys peroxiredoxin from Oryza sativa increases stress tolerance and fermentation capacity in genetically engineered yeast Saccharomyces cerevisiae.

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Peroxiredoxins (Prxs), also termed thioredoxin peroxidases (TPXs), are a family of thiol-specific antioxidant enzymes that are critically involved in cell defense and protect cells from oxidative damage. In this study, a putative chloroplastic 2-Cys thioredoxin peroxidase (OsTPX) was identified by

Glutathione reductase from Oryza sativa increases acquired tolerance to abiotic stresses in a genetically modified Saccharomyces cerevisiae strain.

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Glutathione reductase (GR, E.C. 1.6.4.2) is an important enzyme that reduces glutathione disulfide (GSSG) to a sulfydryl form (GSH) in the presence of an NADPH-dependent system. This is a critical antioxidant mechanism. Owing to the significance of GR, this enzyme has been examined in a number of

Stress response of plant H+-PPase-expressing transgenic Escherichia coli and Saccharomyces cerevisiae: a potentially useful mechanism for the development of stress-tolerant organisms.

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The simple proton-translocating inorganic pyrophosphatase (H(+)-PPase) found in plants and protists is an evolutionally conserved, essential enzyme that catalyzes the hydrolysis of pyrophosphate (PPi). Little is known about the functional contribution of H(+)-PPase to the cellular response to

Rice ASR1 protein with reactive oxygen species scavenging and chaperone-like activities enhances acquired tolerance to abiotic stresses in Saccharomyces cerevisiae.

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Abscisic acid stress ripening (ASR1) protein is a small hydrophilic, low molecular weight, and stress-specific plant protein. The gene coding region of ASR1 protein, which is induced under high salinity in rice (Oryza sativa Ilmi), was cloned into a yeast expression vector pVTU260 and transformed

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