Cloning of peroxisomal ascorbate peroxidase gene from barley and enhanced thermotolerance by overexpressing in Arabidopsis thaliana

Shi, Weiming; Muramoto, Yasunori; Ueda, Akihiro; Takabe, Tetsuko

doi:10.1016/s0378-1119(01)00566-2

Cited by 147 publications

(86 citation statements)

References 20 publications

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“…Other ROS scavenging enzymes have also attracted attention. Catalase over-expression in tobacco resulted in enhanced recovery from high light intensity and MV (Miyagawa et al 2000), while expression of an ascorbate peroxidase gene resulted in protection against aminotriazole (but not paraquat)-induced oxidative stress (Wang et al 1999) and heat stress (Shi et al 2001) in Arabidopsis, and salt and drought stress in tobacco (Badawi et al 2004a). A similar outcome was achieved through the overexpression of glutathione reductase in tobacco (Aono et al 1993) and poplar (Foyer et al 1995).…”

Section: Introductionmentioning

confidence: 90%

Modification of reactive oxygen species scavenging capacity of chloroplasts through plastid transformation

et al. 2011

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Reactive oxygen species (ROS), including superoxide anions, hydrogen peroxide and hydroxyl radicals are generated through normal biochemical processes, but their production is increased by abiotic stresses. The prospects for enhancing ROS scavenging, and hence stress tolerance, by direct gene expression in a vulnerable cell compartment, the chloroplast, have been explored in tobacco. Several plastid transformants were generated which contained either a Nicotiana mitochondrial superoxide dismutase (MnSOD) or an Escherichia coli glutathione reductase (gor) gene. MnSOD lines had a three-fold increase in MnSOD activity, but interestingly a five to nine-fold increase in total chloroplast SOD activity. Gor transgenic lines had up to 6 times higher GR activity and up to 8 times total glutathione levels compared to wild type tobacco. Photosynthetic capacity of transplastomic plants, as measured by chlorophyll content and variable fluorescence of PSII was equivalent to non-transformed plants.The response of these transplastomic lines to several applied stresses was examined. In a number of cases improved stress tolerance was observed. Examples include enhanced methyl viologen (Paraquat)-induced oxidative stress tolerance in Mn-superoxidase dismutase overexpressing plants, improved heavy metal tolerance in glutathione reductase expressing lines, and improved tolerance to UV-B radiation in both sets of plants.

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Section: Introductionmentioning

confidence: 90%

Modification of reactive oxygen species scavenging capacity of chloroplasts through plastid transformation

et al. 2011

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“…Starch granule size, deformed starch granules, and reduced amyloplast numbers are the reported defects of heat stress during post flowering stages [85]. Short-term exposure to heat stress (1 d at 35°C in wheat) results in decreased activity of soluble starch synthase, but further increase in stress duration did not impose any additional impacts [86].…”

Section: Effect Of Heat Stress On Plant Biochemistrymentioning

confidence: 99%

Impacts of Heat Stress on Wheat: A Critical Review

Iqbal¹,

Raja²,

Yasmeen³

et al. 2017

Adv Crop Sci Tech

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A brief review is given of investigations on stress-induced alterations in the yield of different biochemical contents in wheat. Wheat is major cereal crop for fulfilling the calories demands of growing population. Alterations in the worldwide climate are predicted to have critical sentence for crop production. Abiotic stresses such as heat and drought are major abiotic stresses restraining crop production. Heat stress reduces wheat growth by upsetting various physiological and biochemical processes and the developmental stage of the plant is critical in demonstrating the vulnerability of various species and cultivars subjected to high temperature. Heat stress did not affect the protein content but there is strong correlation between leaf nitrogen content and grain protein content. Induction of HSPs seems to be the universal response and adaptation to temperature stress. The synthesis of HSPs is believed to play significant role either in preventing or minimizing the adverse effects of high temperature both at molecular and cellular levels. Wheat has the tendency to adopt diverse types of responses to temperature stress as well as a heat shock by developing thermo-tolerance for the enhancement of the grain quality and yield.

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“…Reactive oxygen byproducts of these processes are removed in part by a membrane-associated ascorbate peroxidase (APX) that cycles electrons through ascorbate to effectively remove hydrogen peroxide and regenerate NAD ϩ (del Río et al, 1998;Corpas et al, 2001;Donaldson, 2002). A peroxisomal isoform of APX has been identified and characterized partially in several different plant species including Arabidopsis (Zhang et al, 1997;Wang et al, 1999), barley (Hordeum vulgare; Shi et al, 2001), cotton (Gossypium hirsutum; Bunkelmann and Trelease, 1996;Mullen et al, 2001b), cucumber (Cucumis sativus; Corpas et al, 1994;Corpas and Trelease, 1998), pea (Pisum sativum; Jiménez et al, 1997;Ló pez-Huertas et al, 1999), pumpkin (Cucurbita pepo; Yamaguchi et al, 1995aYamaguchi et al, , 1995bNito et al, 2001), and spinach (Spinacia oleracea; Ishikawa et al, 1998). Collectively, these studies indicate that peroxisomal APX functions as a singlepass peroxisomal membrane protein (PMP) with its N-terminal active site domain facing the cytosol, where it is thought to scavenge hydrogen peroxide that escapes the peroxisome or that is produced in the cytosol.…”

mentioning

confidence: 99%

“…Zhang et al (1997) determined that peroxisomal AtAPX transcript levels increased slightly in response to various chemical and environmental stresses, and Wang et al (1999) found that tobacco (Nicotiana tabacum) plants overexpressing peroxisomal AtAPX were protected specifically against peroxisome-derived oxidative stress. Although these and another study (Shi et al, 2001) provide important functional information for peroxisomal AtAPX in planta, cell biological aspects related to its posttranslational intracellular sorting and association with organelle membranes have not been elucidated.…”

mentioning

confidence: 99%

Peroxisomal Ascorbate Peroxidase Resides within a Subdomain of Rough Endoplasmic Reticulum in Wild-Type Arabidopsis Cells

2003

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Previously we reported (R.T. Mullen, C.S. Lisenbee, J.A. Miernyk, R.N. Trelease [1999] Plant Cell 11: 2167–2185) that overexpressed ascorbate peroxidase (APX), a peroxisomal membrane protein, sorted indirectly to Bright Yellow-2 cell peroxisomes via a subdomain of the endoplasmic reticulum (ER; peroxisomal endoplasmic reticulum [pER]). More recently, a pER-like compartment also was identified in pumpkin (Cucurbita pepo) and transformed Arabidopsis cells (K. Nito, K. Yamaguchi, M. Kondo, M. Hayashi, M. Nishimura [2001] Plant Cell Physiol 42: 20–27). Here, we characterize more extensively the localization of endogenous Arabidopsis peroxisomal APX (AtAPX) in cultured wild-type Arabidopsis cells (Arabidopsis var. Landsberg erecta). AtAPX was detected in peroxisomes, but not in an ER subcompartment, using immunofluorescence microscopy. However, AtAPX was detected readily with immunoblots in both peroxisomal and ER fractions recovered from sucrose (Suc) density gradients. Most AtAPX in microsomes (200,000g, 1 h pellet) applied to gradients exhibited a Mg2 +-induced shift from a distribution throughout gradients (approximately 18%–40% [w/w] Suc) to ≥42% (w/w) Suc regions of gradients, including pellets, indicative of localization in rough ER vesicles. Immunogold electron microscopy of the latter fractions verified these findings. Further analyses of peroxisomal and rough ER vesicle fractions revealed that AtAPX in both fractions was similarly associated with and located mostly on the cytosolic face of the membranes. Thus, at the steady state, endogenous peroxisomal AtAPX resides at different levels in rough ER and peroxisomes. Collectively, these findings show that rather than being a transiently induced sorting compartment formed in response to overexpressed peroxisomal APX, portions of rough ER (pER) in wild-type cells serve as a constitutive sorting compartment likely involved in posttranslational routing of constitutively synthesized peroxisomal APX.

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Cloning of peroxisomal ascorbate peroxidase gene from barley and enhanced thermotolerance by overexpressing in Arabidopsis thaliana

Cited by 147 publications

References 20 publications

Modification of reactive oxygen species scavenging capacity of chloroplasts through plastid transformation

Modification of reactive oxygen species scavenging capacity of chloroplasts through plastid transformation

Impacts of Heat Stress on Wheat: A Critical Review

Peroxisomal Ascorbate Peroxidase Resides within a Subdomain of Rough Endoplasmic Reticulum in Wild-Type Arabidopsis Cells

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