Evidence for the Presence of the Ascorbate-Glutathione Cycle in Mitochondria and Peroxisomes of Pea Leaves

Jiménez, Ana; Hernández, José Antonio; Rı́o, Luis A. del; Sevilla, Francisca

doi:10.1104/pp.114.1.275

Cited by 744 publications

(534 citation statements)

References 43 publications

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“…Peroxisomes contain enzymatic and nonenzymatic defense mechanisms to deal with different types of ROS such as O 2 .2 and H 2 O 2 . The enzymes involved in these mechanisms include superoxide dismutases, catalase, and components of the ascorbate-glutathione cycle (ascorbate, glutathione, and ascorbate peroxidase as well as dehydroascorbate, monodehydroascorbate, and glutathione reductase; Jiménez et al, 1997;Sandalio and Romero-Puertas, 2015).…”

Section: Discussionmentioning

confidence: 99%

Peroxisomes Extend Peroxules in a Fast Response to Stress via a Reactive Oxygen Species-Mediated Induction of the Peroxin PEX11a

et al. 2016

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Peroxisomes are highly dynamic and metabolically active organelles that play an important role in cellular functions, including reactive oxygen species (ROS) metabolism. Peroxisomal dynamics, such as the proliferation, movement, and production of dynamic extensions called peroxules, have been associated with ROS in plant cells. However, the function and regulation of peroxules are largely unknown. Using confocal microscopy, we have shown that treatment of Arabidopsis leaves with the heavy metal cadmium produces time course-dependent changes in peroxisomal dynamics, starting with peroxule formation, followed by peroxisome proliferation, and finally returning to the normal morphology and number. These changes during Cd treatment were regulated by NADPH oxidase (C and F)-related ROS production. Peroxule formation is a general response to stimuli such as arsenic and is regulated by peroxin 11a (PEX11a), as Arabidopsis pex11a RNA i lines are unable to produce peroxules under stress conditions. The pex11a line showed higher levels of lipid peroxidation content and lower expression of genes involved in antioxidative defenses and signaling, suggesting that these extensions are involved in regulating ROS accumulation and ROSdependent gene expression in response to stress. Our results demonstrate that PEX11a and peroxule formation play a key role in regulating stress perception and fast cell responses to environmental cues.Peroxisomes are highly versatile organelles that adapt to changes in their cellular environment through morphological and metabolic adjustments (Hu et al., 2012;Sandalio et al., 2013). Plant peroxisomes perform essential functions such as photorespiration and fatty acid b-oxidation, ureide, and phytohormone (auxin and jasmonic acid) metabolisms, and also act as a source of signal molecules such as reactive oxygen and nitrogen species (ROS and RNS; Sandalio and RomeroPuertas, 2015). Peroxisomes contain a large battery of antioxidants to control ROS and RNS accumulation (Sandalio and Romero-Puertas, 2015). These organelles proliferate in response to environmental cues through a complex process involving elongation, constriction, and fission (Hu et al., 2012;Baker and Paudyal, 2014). Deciphering the signaling pathways governing the regulation of peroxisome proliferation under different environmental and metabolic conditions presents a major challenge in this field of research. Before peroxisomal division, organelle elongation occurs in a process regulated by peroxins 11 (PEX11), with the final division requiring dynamin-like or dynamin-related proteins and fission proteins (Hu et al., 2012, Schrader et al., 2012. There is evidence to suggest that ROS are involved in regulating peroxisome proliferation, as some peroxisomal biogenesis genes (PEX) are transcriptionally regulated by H 2 O 2 in both plant and animal cells (López-Huertas et al., 2000). The formation of peroxisomal extensions, known as peroxules, has also been observed to be regulated by exogenous applications of H 2 O 2 (Sinclair et al., 2009;Ba...

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Section: Discussionmentioning

confidence: 99%

Peroxisomes Extend Peroxules in a Fast Response to Stress via a Reactive Oxygen Species-Mediated Induction of the Peroxin PEX11a

et al. 2016

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“…Monodehydroascorbate reductase is ubiquitous in all the phylogenetic groups and its isoforms existing in chloroplasts (Hossain et al 1984), cytosol (Dalton et al 1993), peroxisomes and mitochondria (Jimenez et al 1997) have been reported. The activity of MDAR has been shown to be up-regulated under several stress conditions, for instance in tomato by salinity stress (Mittova et al 2003) and high light intensity (Gechev et al 2003), in rice by low temperature (Oidaira et al 2000), and in Arabidopsis by UV-C exposure (Kubo et al 1999).…”

Section: Introductionmentioning

confidence: 99%

Oxidative stress induced expression of monodehydroascorbate reductase gene in Eleusine coracana

Sudan

Negi

Arora

2015

Physiol Mol Biol Plants

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Abiotic stresses constitute a serious threats to the world food security as they cause significant economic losses in terms of reduction in crop productivity and also greatly limit the geographical locations where crops can be grown. Exposure to abiotic stress causes over-production of reactive oxygen species, leading to oxidative stress in plants. Induction of oxidative stress is primarily responsible for a variety of detrimental changes in the cellular physiology. However, plants have evolved intricate anti-oxidative defence machinery, for their survival under stress. Plant defence strategies for stress tolerance rely on the expression of anti-oxidative genes required for scavenging the toxic reactive oxygen species. Monodehydroascorbate reductase is one of the key anti-oxidant enzyme responsible for scavenging reactive oxygen species. In the present study, efforts have been made to understand the role of monodehydroascorbate reductase in finger millet under different abiotic stresses (drought, salt and UV radiation). The study establishes a differential link between mdar gene expression and enzyme activity under oxidative stress that is validated under different types of imposed stresses. Alteration in correlation between gene expression and enzyme activities under varying magnitude of oxidative stress is elucidated.

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“…This fact is of some importance since the expected increase in H # O # as a result of the SOD reaction was accompanied by an increased enzymatic capacity to decompose it. Considering that in pea leaves most of the ASC-GSH cycle enzymes is between chloroplasts and cytosol (Gillham & Dodges 1986 ;Edwards et al, 1990 ;Mittler & Zilinskas, 1994 ;Jime! nez et al, 1997a), our results suggest that in NaCl-treated leaves and in both cell compartments, the N # O # generated by increased FeSOD and CuZn-SODs I and II could be removed by APX and MDHAR.…”

Section:   mentioning

confidence: 99%

Response of antioxidant systems and leaf water relations to NaCl stress in pea plants

et al. 1999

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A pea (Pisum sativum cv. Puget) cultivar was grown on a medium containing different NaCl concentrations (0-160 mol m −$ ) in order to study the effects of salt stress on leaf water relations and on the activity of antioxidant enzymes. NaCl stress caused a rapid decline in chlorophyll content. Both leaf water (ψ l ) and osmotic potentials (ψ s ) decreased progressively with the severity of the stress (from 90-160 mol m −$ NaCl) whereas leaf turgor pressure (ψ p ) increased in treated plants. Pea leaves contained an iron-containing superoxide dismutase (Fe-SOD) isozyme in chloroplasts alongside a copper-zinc-containing (CuZn-SOD) form (CuZn-SOD II). The lowest NaCl concentration (70 mol m −$ ) had no effect on the activity of these antioxidant enzymes while higher concentrations (110-130 mol m −$ ) enhanced the activity of cytosolic CuZn-SOD I and chloroplastic CuZn-SOD II as well as that of mitochondrial and\or peroxisomal manganese-containing superoxide dismutase (Mn-SOD). These inductions were matched by increases in the activity of ascorbate peroxidase (APX) and monodehydroascorbate reductase (MDHAR). The increased activities coincided with decreased stomatal conductance and were unaffected by the severity of stress except in the case of CuZn-SOD II which fell to control values under the highest stress conditions (140-160 mol m −$ NaCl), when a concomitant increase in chloroplastic Fe-SOD activity was observed. Glutathione reductase (GR) and dehydroascorbate reductase (DHAR) activities were only induced under severe NaCl stress (130-160 mol m −$ ) and were accompanied by losses in the ascorbate and glutathione pools, lower ASC\DHA and GSH\GSSG ratios and increases in GSSG. Electron microscopy showed that the thylakoidal structure of the chloroplasts became disorganized and their starch content decreased in plants treated with 160 mol m −$ NaCl. Overall, the results suggest that salt stress is accompanied by oxidative stress, perhaps at the cell compartment level. The capacity of Puget cultivar to ensure cell turgor and to enhance the activity of enzymes involved in the defence against oxidative stress seems to be important in determining adaptation to moderate NaCl stress conditions. In plants exposed to severe NaCl stress (130-160 mol m −$ ) it seems that such resistance to oxidative stress is overcome, which might contribute to the deleterious effects of salt and significant growth reduction in these conditions.

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Evidence for the Presence of the Ascorbate-Glutathione Cycle in Mitochondria and Peroxisomes of Pea Leaves

Cited by 744 publications

References 43 publications

Peroxisomes Extend Peroxules in a Fast Response to Stress via a Reactive Oxygen Species-Mediated Induction of the Peroxin PEX11a

Peroxisomes Extend Peroxules in a Fast Response to Stress via a Reactive Oxygen Species-Mediated Induction of the Peroxin PEX11a

Oxidative stress induced expression of monodehydroascorbate reductase gene in Eleusine coracana

Response of antioxidant systems and leaf water relations to NaCl stress in pea plants

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