<i>Arabidopsis</i> glutathione‐dependent formaldehyde dehydrogenase is an <i>S</i>‐nitrosoglutathione reductase

Sakamoto, Atsushi; Ueda, Mitsutoshi; Morikawa, Hiromichi

doi:10.1016/s0014-5793(02)02414-6

Cited by 211 publications

(143 citation statements)

References 24 publications

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“…Among the analyzed eight independent transgenic lines, all plants showed a phenotype similar to that of wild type, including the restored sensitivity to paraquat and normal growth and development ( Figure 3C and data not shown), suggesting that the observed par2-1 mutant phenotype was caused by a mutation in At5g43940. In previous studies, At5g43940 has been characterized to encode a GSNOR [41,42,44,45]. A loss-of-function mutation in GSNOR1 (gsnor1-3) caused no GSNOR1 transcript accumulation [42], thus likely representing a null mutation (see Figure 3A).…”

Section: Molecular Cloning Of Par2mentioning

confidence: 99%

“…GSNOR1 is a single-copied gene in Arabidopsis, and has been characterized in some detail [41][42][43][44][45][46]. Loss-or gain-of-function mutations in GSNOR1 caused altered innate immunity against a variety of pathogens and altered intracellular SNO levels [42,43].…”

Section: Par2 Encodes An Gsnormentioning

confidence: 99%

“…In Arabidopsis, the single-copied GSNOR1 gene has been genetically and biochemically characterized [41][42][43][44][45][46][47]. Recombinant Arabidopsis GSNOR1 protein shows enzymatic activity of reducing GSNO in vitro [45].…”

Section: Introductionmentioning

confidence: 99%

“…Recombinant Arabidopsis GSNOR1 protein shows enzymatic activity of reducing GSNO in vitro [45]. Moreover, mutations in GSNOR1 cause developmental defects and altered responses to both biotic and abiotic stresses [42,46].…”

Section: Introductionmentioning

confidence: 99%

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The Arabidopsis PARAQUAT RESISTANT2 gene encodes an S-nitrosoglutathione reductase that is a key regulator of cell death

et al. 2009

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Metabolism of S-nitrosoglutathione (GSNO), a major biologically active nitric oxide (NO) species, is catalyzed by the evolutionally conserved GSNO reductase (GSNOR). Previous studies showed that the Arabidopsis GSNOR1/ HOT5 gene regulates salicylic acid signaling and thermotolerance by modulating the intracellular S-nitrosothiol level. Here, we report the characterization of the Arabidopsis paraquat resistant2-1 (par2-1) mutant that shows an anti-cell death phenotype. The production of superoxide in par2-1 is comparable to that of wild-type plants when treated by paraquat (1,1′-dimethyl-4,4′-bipyridinium dichloride), suggesting that PAR2 acts downstream of superoxide to regulate cell death. PAR2, identified by positional cloning, is shown to be identical to GSNOR1/HOT5. The par2-1 mutant carries a missense mutation in a highly conserved glycine, which renders the mutant protein unstable. Compared to wild type, par2-1 mutant has a higher NO level, as revealed by staining with 4,5-diaminofluorescein diacetate. Consistent with this result, wild-type plants treated with an NO donor display resistance to paraquat. Interestingly, the GSNOR1/HOT5/PAR2 protein level, other than its steady-state mRNA level, is induced by paraquat, but is reduced by NO donors. Taken together, these results suggest that GSNOR1/HOT5/PAR2 plays an important role in regulating cell death in plant cells through modulating intracellular NO level.

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Section: Molecular Cloning Of Par2mentioning

confidence: 99%

Section: Par2 Encodes An Gsnormentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The Arabidopsis PARAQUAT RESISTANT2 gene encodes an S-nitrosoglutathione reductase that is a key regulator of cell death

et al. 2009

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“…Furthermore, it has been demonstrated recently that it is very active in the reduction of S-nitrosoglutathione, the condensation product of glutathione and NO (Jensen et al, 1998;Liu et al, 2001;Sakamoto et al, 2002).…”

mentioning

confidence: 99%

Enhanced Formaldehyde Detoxification by Overexpression of Glutathione-Dependent Formaldehyde Dehydrogenase from Arabidopsis

et al. 2003

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The ADH2 gene codes for the Arabidopsis glutathione-dependent formaldehyde dehydrogenase (FALDH), an enzyme involved in formaldehyde metabolism in eukaryotes. In the present work, we have investigated the potential role of FALDH in detoxification of exogenous formaldehyde. We have generated a yeast (Saccharomyces cerevisiae) mutant strain (sfa1⌬) by in vivo deletion of the SFA1 gene that codes for the endogenous FALDH. Overexpression of Arabidopsis FALDH in this mutant confers high resistance to formaldehyde added exogenously, which demonstrates the functional conservation of the enzyme through evolution and supports its essential role in formaldehyde metabolism. To investigate the role of the enzyme in plants, we have generated Arabidopsis transgenic lines with modified levels of FALDH. Plants overexpressing the enzyme show a 25% increase in their efficiency to take up exogenous formaldehyde, whereas plants with reduced levels of FALDH (due to either a cosuppression phenotype or to the expression of an antisense construct) show a marked slower rate and reduced ability for formaldehyde detoxification as compared with the wild-type Arabidopsis. These results show that the capacity to take up and detoxify high concentrations of formaldehyde is proportionally related to the FALDH activity in the plant, revealing the essential role of this enzyme in formaldehyde detoxification.

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Reactive Oxygen Species and Nitric Oxide Production, Regulation and Function During Defense Response

Molina‐Moya

Terrón-Camero

Pescador‐Azofra

et al. 2019

Reactive Oxygen, Nitrogen and Sulfur Species in Plants

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Arabidopsis glutathione‐dependent formaldehyde dehydrogenase is an S‐nitrosoglutathione reductase

Cited by 211 publications

References 24 publications

The Arabidopsis PARAQUAT RESISTANT2 gene encodes an S-nitrosoglutathione reductase that is a key regulator of cell death

The Arabidopsis PARAQUAT RESISTANT2 gene encodes an S-nitrosoglutathione reductase that is a key regulator of cell death

Enhanced Formaldehyde Detoxification by Overexpression of Glutathione-Dependent Formaldehyde Dehydrogenase from Arabidopsis

Reactive Oxygen Species and Nitric Oxide Production, Regulation and Function During Defense Response

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