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physcomitrella patens/detox

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A SABATH Methyltransferase from the moss Physcomitrella patens catalyzes S-methylation of thiols and has a role in detoxification.

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Known SABATH methyltransferases, all of which were identified from seed plants, catalyze methylation of either the carboxyl group of a variety of low molecular weight metabolites or the nitrogen moiety of precursors of caffeine. In this study, the SABATH family from the bryophyte Physcomitrella
The ascorbate-glutathione pathway plays a major role in the detoxification of reactive oxygen species (ROS) in vascular plants. One of the key enzymes in this pathway is monodehydroascorbate reductase (MDHAR), a FAD enzyme that catalyses the reduction of the monodehydroascorbate radical. To

The Physcomitrella patens Chloroplast Proteome Changes in Response to Protoplastation.

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Plant protoplasts are widely used for genetic manipulation and functional studies in transient expression systems. However, little is known about the molecular pathways involved in a cell response to the combined stress factors resulted from protoplast generation. Plants often face more than one

Modified suppression subtractive hybridization identifies an AP2-containing protein involved in metal responses in Physcomitrella patens.

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The moss Physcomitrella patens has two life cycles, filamentous protonema and leafy gametophore. A modified from of suppression subtractive hybridization (SSH), mirror orientation selection (MOS), was applied to screen genes differentially expressed in the P. patens protonema. Using reverse Northern

Proteome analysis of gametophores identified a metallothionein involved in various abiotic stress responses in Physcomitrella patens.

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Physcomitrella patens is a model plant for studying gene function using a knockout strategy. To establish a proteome database for P. patens, we resolved over 1,500 soluble proteins from gametophore and protonema tissues by two-dimensional electrophoresis (2-DE) and obtained peptide mass fingerprints

Degradation of glutathione S-conjugates in Physcomitrella patens is initiated by cleavage of glycine.

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Glutathione-dependent detoxification is a key pathway that allows plants to efficiently remove toxic compounds like heavy metals or electrophilic xenobiotics. Under persistent exposure to toxins plants need to respond to continuous demand with efficient synthesis of glutathione (GSH) and ideally

PpAKR1A, a Novel Aldo-Keto Reductase from Physcomitrella Patens, Plays a Positive Role in Salt Stress.

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The moss Physcomitrella patens is tolerant of highly saline environments. In plants, salinity stress may induce the production of toxic reactive carbonyl species (RCS) and oxidative damage. Aldo-keto reductases (AKRs) are a large group of NADP-dependent oxidoreductases involved in RCS

Chloroplasts Require Glutathione Reductase to Balance Reactive Oxygen Species and Maintain Efficient Photosynthesis.

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Thiol-based redox-regulation is vital to coordinate chloroplast functions depending on illumination and is well investigated for thioredoxin-dependent processes. In parallel, glutathione reductase (GR) maintains a highly reduced glutathione pool, enabling glutathione-mediated redox buffering. Yet,
Plant glutathione S-transferases (GSTs) are multifunctional proteins encoded by a large gene family that play major roles in the detoxification of xenobiotics and oxidative stress metabolism. To date, studies on the GST gene family have focused mainly on vascular plants (particularly agricultural
Physcomitrella patens contains four metallothionein-like genes. Three were shown to confer metal tolerance in yeast. Transcript profiling suggests their roles in senescence and reproductive development or cadmium and oxidative stress. Metallothioneins (MTs) have been suggested to play various roles
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