Plant Gene 19 (2019) 100182

Contents lists available at ScienceDirect

Plant Gene
journal homepage: www.elsevier.com/locate/plantgene

Antioxidant enzymes regulation in plants in reference to reactive oxygen T

species (ROS) and reactive nitrogen species (RNS)
Dhriti Kapoora,1, Simranjeet Singhb,c,d,1, Vijay Kumare,1, Romina Romerof, Ram Prasadg,h, ,
⁎⁎

Joginder Singhb,
⁎

a
Department of Botany, Lovely Professional University, Phagwara, Punjab, India
b
Department of Biotechnology, Lovely Professional University, Phagwara, Punjab, India
c
Regional Advanced Water Testing Laboratory (RAWTL), Mohali, India
d
Punjab Biotechnology Incubators, Mohali, Punjab 160059, India
e
Regional Ayurveda Research Institute for Drug Development, Gwalior, MP, India
f
Technological Development Unit-UDT, Universidad de Concepcion, Cordillera 2634, 4191996, Box 4051, Coronel, Chile
g
School of Environmental Science and Engineering, Sun Yat-Sen University, Guangzhou 510006, China
h
Amity Institute of Microbial Technology, Amity University, Noida 201313, India

ARTICLE INFO ABSTRACT

Keywords: Reactive oxygen species (ROS) are generated in the plants during cellular metabolism. But extreme environ-
Reactive oxygen species mental conditions like drought, salinity or floods etc. lead to an enhanced level of these ROS in plants, which
Reactive nitrogen species cause deterioration of lipids, proteins and nucleic acids and ultimately death of a plant. Growing evidence has
ascorbic acid suggested that ROS play a critical role as the signaling molecules throughout the entire cell death pathway.
glutathione
Though ROS act as a signalling molecule, but they can cause oxidative burst if there is an imbalance between
oxidative stress
ROS generation and their scavenging. Apart from these ROS, nitrogen species (RNS) also play a significant role in
causing oxidative damage and tissue dysfunction and act as molecular signals. Consequently, cells develop a
balanced system to counteract the effect of ROS, such as antioxidative defense system comprises enzymatic
antioxidant enzymes like superoxide dismutase, catalase, glutathione peroxidases etc. and non-enzymatic an-
tioxidants which cooperatively reduce oxidative state. Herein, we review the novel findings of cellular processes
induced by ROS and RNS and recapitulate the functions of cellular endogenous antioxidant systems as well as
natural anti-oxidative compounds in plants to facilitate the illustration of the imperative role of antioxidants in
prevention against oxidative stress.

1. Introduction
In the biological system, oxidative stress is a natural physiological
process where the presence of free oxygen radicals overpowers the ra-
dical scavenging strategies that lead to an imbalance between the re-
active oxygen species and the antioxidants (Foyer and Harbinson,
1994). Oxidative stress is a state of enhanced levels of reactive oxygen
species (ROS), which is also called “oxidants” or “oxygen-derived spe-
cies”. The function is regulated physiologically by the level of oxygen,
signal transduction, and preservation of redox homeostasis. The redox
regulation is a hastily rising field of research that has an influence on
nearly all the spheres including biological systems which have devel-
oped strategies of utilizing oxidants to their benefit and also modified to
the coexistence of detrimental free radicals. Both ROS and reactive
nitrogen species (RNS) are generated in a well-controlled way to assist
regulation of homeostasis at the cellular level in the normal healthy
tissues and contribute significantly as second messengers, and control
cellular activity by modulating signaling pathways (Nath et al., 2016,
2017, 2018).
An oxidant is defined as a molecule which contains one or more
unpaired electrons and acts as an oxidizing agent during the redox re-
action. It triggers the production of free radicals by transferring an
electron in a chemical reaction. Oxygen is utilized by the cells for
generating energy and free radicals, which are the result of ATP pro-
duction by the mitochondria (Blokhina and Fagerstedt, 2010). Being a
part of propagative chain reaction, free radicals combine with other

⁎
Correspondence to: J. Singh, Department of Biotechnology, Lovely Professional University, Phagwara, Punjab, India.
⁎⁎
Correspondence to: R. Prasad, School of Environmental Science and Engineering, Sun Yat-Sen University, Guangzhou 510006, China.
E-mail addresses: prasad@mail.sysu.edu.cn (R. Prasad), joginder.15005@lpu.co.in (J. Singh).
1
Equal contribution

https://doi.org/10.1016/j.plgene.2019.100182
Received 25 October 2018; Received in revised form 3 March 2019; Accepted 23 April 2019
Available online 24 April 2019
2352-4073/ © 2019 Elsevier B.V. All rights reserved.
D. Kapoor, et al.
radicals and become more deteriorative, till the chain is not stopped by
antioxidants, which are chain breaking substances and nontoxic in
nature (Heyno et al., 2011).
All organisms possess intrinsic cellular defences to combat oxidative
stress; those substances are termed as antioxidants. Free radicals have a
short life span, like in milli, micro, or nanoseconds, and they voluntarily
react with lipids, DNA, proteins etc. and causing damage and form
harmful products such as lipid peroxides and other lipid adducts. The
resulting protein damage causes a reduction in enzyme activities, while
DNA leads to mutagenesis and carcinogenesis (Shah et al., 2001). In the
biological systems, the subsistence of these oxidants at the beginning of
the 20th century was discovered in 1954 (Foyer and Harbinson, 1994).
Gerschman et al. (2001) analyzed that the lethal effects of X- irradiation
and hyperbaric oxygen had a widespread mechanism that included
radical and non-radical species, resulting from the partial decrease of
oxygen (Del et al., 2006). These species, at present, referred to as re-
active oxygen species (ROS) and might play a role in the ageing process
(Blokhina and Fagerstedt, 2010). Then in 1969, the enzy-me superoxide
dismutase (SOD) was isolated which further leads to improvement in
the free radical knowledge (Heyno et al., 2011). Discovery of the SOD
encouraged a large number of studies, which enhanced the knowledge
of the ROS. Although for several years they were supposed to be having
solely harmful effects. These findings indicated that ROS readily react
with most biological macromolecules and leads to their oxidative
modification and consequently resulting in the loss of their activities
(Shah et al., 2001). Essentially ROS include species, such as the hy-
droxyl radical (∙OH), a very reactive species as it reacts very close to its
site of generation (Mittler, 2002), and other species, like hydrogen
peroxide (H2O2) and superoxide (O2∙−) are less reactive. Thus, ni-
trogen-containing species, which are at present known as reactive ni-
trogen species (RNS), including nitric oxide (NO∙), that is comparatively
unreactive, and its derivative namely peroxynitrite (ONOO−), is a
prevailing oxidant, able to cause damage to various biological mole-
cules (Sharma and Dubey, 2005). This review contains a brief discus-
sion about the different Antioxidant systems (enzymatic and non-en-
zymatic), sources of ROS and RNS, their generation system, and
molecular mechanism behinds its regulation which facilitate the im-
perative role of antioxidants in prevention against different oxidative
stress.
2. Antioxidant systems (enzymatic and non-enzymatic) in plants
The oxidation of protein by covalent interaction is induced either by
reactive oxygen species or byproducts of oxidative stress (Forrester
et al., 2018; Krumova and Cosa, 2016; Gill and Tuteja, 2010). Most
kinds of protein oxidations are basically irreversible, while sulphur
containing amino acids are reversible (Ahmad et al., 2017). It is
widespread and commonly used as a marker for ROS or oxidative stress
(Pisoschi and Pop, 2015). It has been well documented that ROS in-
terfere with signal transduction pathways and plays a functional role as
secondary messengers (Hossain et al., 2015). The hazardous effects of
oxidative stress and reactive oxygen species are countered by both
enzymatic and non-enzymatic antioxidative system such as ascorbate
peroxidase (APX) (Sharma et al., 2016), ascorbic acid (AsA) (Foyer,
2017), catalase (CAT) (Furukawa et al., 2017), glutathione (Diaz-
Vivancos et al., 2015), glutathione reductase (GR) (Lushchak, 2014),
phenolic compounds superoxide dismutase (SOD) (Bresciani et al.,
2015) and tocopherol (Birben et al., 2012). Genetic engineering ap-
proaches have given significant results in terms of refining tolerance to
a multitude of abiotic stresses by heightened activities of non-enzymatic
and enzymatic antioxidant (Birnie-Gauvin et al., 2017).
Although, every cellular compartment such as cytosol contains one
or more enzymatic activity that scavenges hydrogen peroxide (PrxR,
GPX and APX) (Cha et al., 2014). Development in genetic engineering
led to the overexpression of genes which are an option to produce stress
tolerant plants (Ha et al., 2012). Various antioxidants enzymes such as
2
Plant Gene 19 (2019) 100182
Superoxide dismutase, Catalases, Glutathione peroxidases, Ascorbate
peroxidase, Glutathione reductase and non-enzymatic antioxidants such
as α-Tocopherols, ascorbic acid, Glutathione and carotenoids plays an
crucial role in combating the oxidative stress caused by various abiotic
stress and plays a critical role in its survival (Sisein, 2014; Nath et al.,
2016, 2017, 2018). Out of these, an enzymatic antioxidant such as
catalases is also reported to dismutate Hydrogen peroxidase which is
essential for detoxification of ROS during stress (Sharma et al., 2012).
The proliferation of peroxisomes plays an indispensable in scavenging
hydrogen peroxide which diffuses from the cytosol of the cell (Nordgren
and Fransen, 2014). An increase in catalase helps in reducing hazardous
effects of hydrogen peroxide to overcome the mutilation of tissue me-
tabolism (R-Ramis et al., 2015). The up-regulation of superoxide dis-
mutase is implicated in contending oxidative stress caused due to var-
ious abiotic stresses and plays an indispensable role in plant survival.
Various studies confirmed that during stress conditions, increase in
Superoxide dismutase was observed which scavenges cytotoxic hy-
drogen peroxide and helps in the survival of plants (Biczak, 2016).
Multiple isozymes such as Glutathione peroxidases are also reported to
reduce the cytotoxic hydroperoxides and hydrogen peroxide to alcohols
(Boguszewska and Zagdańska, 2012). Glutathione peroxidases also
serve to reclaim lipid peroxidation which is formed during ROS (Chen
et al., 2012). Another antioxidant enzyme Ascorbate peroxidase is also
well documented which involves in scavenging of hydrogen peroxide
ascorbate–glutathione cycles utilizing AsA as the electron donor
(Sharma et al., 2012).
Non-enzymatic antioxidants, such as carotenoids pigments (β-car-
otene) reacts with hydroxyl, superoxide and peroxyl radicals resulting
in pro-oxidant effects at elevated oxygen concentrations (Carocho and
Ferreira, 2013). Both retinoic acid and carotenoids have the potential to
regulate transcription factors (Sharoni et al., 2012). Carotenoids hinder
the activation of tumour necrosis factor-α production, oxidation in-
duced NF-κB and interleukin (IL)-6 (Ferretti et al., 2012). β-carotene
also disrupts apoptosis. Recent studies reveal the anti-proliferative da-
mage of retinoic acid in plants is mediated by acid receptors and it also
triggers apoptosis or by inducing cell arrest (Alizadeh et al., 2014).
Glutathione (GSH) plays a main role in the antioxidative defense system
by stimulating ascorbic acid, through the Ascorbate–Glutathione cycle
(Wang et al., 2012a, b). GSH plays a central role in several physiolo-
gical processes, including conjugation of metabolites, signal transduc-
tion, expression of stress-responsive genes, regulation of sulphate
transport, and detoxification of xenobiotics (Zagorchev et al., 2013). As
an oxidant Glutathione functions in utilization to reduce dehy-
droascorbate (DHA) both enzymatically and non-enzymatically and
oxidized to glutathione disulfide (GSSG) (Das and Roychoudhury,
2014). The regeneration is catalyzed by glutathione reductase to con-
vert GSSG to GSH (Glutathione) using NADPH as reducing power
(Deponte, 2013). The high reductive potential of Glutathione is due to
the nucleophilic cysteine residue. It reacts with superoxide radicals,
hydroxyl radicals and singlet oxygen non-enzymatically to scavenge
cytotoxic hydrogen peroxide (Forman et al., 2014).
3. Sources of ROS and RNS
With the enhancement of oxygen-evolving photosynthesis by the
plants, atmospheric oxygen levels rose on earth approx. 2.4 billion
years ago, that resulted in the great oxidation event (Inupakutika et al.,
2016). That further cause increase in the two processes including life on
the planet: Among them, first is the evolution of physiological me-
chanisms that generate energy by utilizing oxygen; this phenomenon
also termed as oxidative phosphorylation and the second one is the
development of defensive strategies against oxygen burst. With in-
creasing complexity, plants developed strategies to combat the effects
of reactive oxygen species. It has been reported by Inupakutika et al.
(2016) that the evolution of ROS metabolism has evolved as 3.6 billion
years ago, which came to existence as the great oxidation event. Free
D. Kapoor, et al.
radicals are generally a chemical species with one or more unpaired
electrons. Almost all these pro-oxidants originated from O2. However,
there are certain other reactive molecules which are supposed to ori-
ginate from other elements, like nitrogen, which is termed as RNS
(reactive nitrogen species). ROS/RNS generated from various chemical
reactions occurring in different compartments in case of plants, such as
during respiration in mitochondria, photosynthesis in chloroplasts,
oxidation-reduction reactions in the cytosol and cellular photorespira-
tion in peroxisomes.
It is a well-known fact that in growth and development, nutrient
sensing, reproduction, and defensive responses to ameliorate biotic and
abiotic factors, ROS and RNS play significant roles in various signalling
pathways, in which they are foremost involved in redox regulation of
thiols on proteins. Consequently, proteins that can contribute in the
regulation of thiols or use them as reducing power- for example glu-
taredoxins, thioredoxins, sulfiredoxin, peroxiredoxins etc. have been
the focus of research, (Waszczak et al., 2015; Sevilla et al., 2015).
Generation of ROS and RNS due to various biotic factors lead to
oxidative damage to tissue and resulting deterioration and sometimes
impaired removal of these species may result in adverse effects to
plants. Mitochondria are the site for the production of oxidative energy.
From various biosynthetic reaction pathways in aerobic cells, it is found
out that any type of mitochondrial dysfunction may cause impaired cell
function and development of several abnormalities. There is a large
number of information available on mitochondrial ROS generation and
cause of oxidative burst and deteriorations in functions due to mi-
tochondrial ROS (Pacher et al., 2007). On the other hand, the reports
also suggest that mitochondria are not the root cause for the dysfunc-
tioning of tissue during oxidative stress. Cellular abnormalities or de-
teriorations have been stimulated by an enhanced level of reactive
oxygen species. Organelle-specific ROS measurements can be made by
the use of fluorescent protein-based probes for H2O2 and GSH/GSSG
redox state now days. Still, there is a scarcity of information regarding
the various sources of these free radicals which are responsible for
causing the oxidative damage (Stohs and Bagchi, 1995).
4. Production and functions of ROS in plants
Reactive oxygen species became an indispensable part of aerobic life
with the introduction of molecular oxygen by photosynthetic organisms
evolving O2 directly into the atmosphere (Taverne et al., 2018; Gupta
et al., 2017; Schmitt et al., 2016). The reactive oxygen species are a part
of the normal metabolism of the cell, but the deleterious effect of the
same materializes when the balance between the ROS produced and
ROS scavenged is disturbed (Tiwari et al., 2017; Sewelam et al., 2016;
Olson and Straub, 2015). ROS plays an important role in various de-
velopmental processes by acting as signalling molecules, programmed
cell death, acclimation, acquired resistance and in hypersensitive re-
action as defense response (Dunnill et al., 2017; Di Meo et al., 2016;
Reczek and Chandel, 2015). The reduction or activation of molecular
oxygen forms reactive oxygen species which includes hydroxyl radical
(HO), hydrogen peroxide (H2O2) and singlet oxygen (1O2) (Choudhury
et al., 2017; Krumova and Cosa, 2016; del Río, 2015). Reactive oxygen
species are generated as side products of various biochemical pro-
cesses/reactions and are regularly generated in apoplast, cytosol, mi-
tochondria, peroxisomes and plastids (Mittler, 2017; Qi et al., 2017;
You and Chan, 2015; Karkonen and Kuchitsu 2015). In the oxidizing
environment, most of the plants regularly produce reactive oxygen
species in peroxisomes, chloroplasts, mitochondria and other parts of
cell due to their metabolic processes like respiration photosynthesis etc
(Del Río and López-Huertas, 2016; Huang et al., 2016a, b; Sandalio and
Romero-Puertas, 2015; Petrov et al., 2015). Various environmental
stresses such as pathogen attack, low or high temperature, nutrient
deficiency, salinity, drought, high or low temperature and high light
trigger the generation of reactive oxygen species in plants (Hossain
et al., 2015; Ramegowda and Senthil-Kumar, 2015). Pesticides also
3
Plant Gene 19 (2019) 100182
induce production of reactive oxygen species and depletion of anti-
oxidants (Singh et al., 2017a, Singh et al., 2016, Singh et al., 2017b).
Upon damage to this equilibrium, accumulation of ROS can affect cell
growth and survival (Adrees et al., 2015).
A host of antioxidant and oxidant, and other small molecules pre-
sent in the various plant species dissipates reactive oxygen species
(Espinosa-Diez et al., 2015; Poole et al., 2015). The imbalance between
the production of reactive oxygen species and their detoxification by
non-enzymatic & enzymatic reaction causes oxidative stress which
causes photo-oxidative damage to proteins, lipids, DNA and eventually
cell death (Jha and Subramanian, 2016; Demidchik, 2015; Gill et al.,
2015). Disturbance of cellular function and removal of electrons from
organic molecules are caused by the presence of elevated concentra-
tions of oxidizing agents via oxidative stress mechanism (Pisoschi and
Pop, 2015; Bhat et al., 2015). Increased concentration of ROS produc-
tion leads to cell death by inducing ROS activated cell death signalling
events (Schenk and Fulda, 2015; Gong et al., 2015). Partial reduction or
activation of unreactive di-oxygen molecule results in the formation of
reactive oxygen species in the form of HO, H2O2 and 1O2 (Gupta et al.,
2015; Anjum, 2015; Nakabayashi and Saito, 2015). Plant cell organelles
such as mitochondria, peroxisomes chloroplast etc and enzymes such as
amine oxidases and peroxidases with a high rate of electron flow or
high oxidizing metabolic activity are the major sources of ROS pro-
duction in response to stress signalling (Choudhury et al., 2017; Kapoor
et al., 2015). Oxygen production in the stroma of chloroplasts is a
continuous process in the photosynthetic electron transport system and
it is removed by assimilation and reduction process (Takagi et al., 2016;
Corpas et al., 2015). Reduction process involves photons which reduce
electron transport components to superoxide radical which finally
linked a reaction in the photo-respiratory system of the plant (Gautam
et al., 2017; Huang et al., 2016a, b). Due to various environmental
stresses, the availability of carbon dioxide inside the leaves is restricted,
ribulose-1,5-bisphosphate oxygenase/carboxylase initiates a reaction in
which O2 is utilized over deficiency of CO2 which leads to the formation
of glycolate after oxidation by glycolate oxidase which further moves to
peroxisomes and generate H2O2 (Bloom, 2015; Hao et al., 2015). In
Plasma membrane, a multimeric flavocytochrome forms an electron
transport chain which reduces di-molecule oxygen to reactive oxygen
moiety using NADPH dependent oxidases (Tomar et al., 2017; O’Neill
et al., 2015). In apoplast of the cell, amine oxidase, oxalate oxidase and
pH-dependent cell wall peroxidase are reported to produce ROS using
reduction mechanism (Mittler, 2017; Qi et al., 2017; You and Chan,
2015).
5. RNS generation and functions in plants
Due to the action of enzyme nitric oxide synthase, there is a gen-
eration of NO in an animal system. In a complex reaction, nitric oxide
synthase increases the rate of reaction of NADPH dependent and oxygen
of l-arginine to citrulline and NO, using calmodulin, Ca2+, (BH4) FAD,
tetrahydrobiopterin and FMN (del Rio 2015). A study conducted by
Foresi et al. (2010) reported that Ostreoccus tauri (marine green alga) is
the only species to produce NOS in the plant kingdom. The Sequence
length of species showed a similarity index of 43, 42 and 34 per cent
with iNOS, eNOS and nNOS (Foresi et al., 2010). In plants, there are
non-enzymatic and enzymatic systems which are the potent source of
NO (Mur et al., 2013; Hancock, 2012). Moreover, various data related
to l-arginine-dependent NOS activity in the extracts of different species
of plants have also been documented (del Río, 2015). Very less in-
formation about the sub-cellular site of NO production in plant system
is available till date. The NOS activity was observed in the peroxisomes
organelle in plant tissues (Luis and Río, 2013). In addition to peroxi-
somes, organelles like chloroplast (Jasid et al., 2006) and mitochondria
(Gupta and Kaiser, 2010) have been reported which generates NO.
Nitric oxide performs an important role, in intra and intercellular
signalling and growth and development of plants. They have multiple
D. Kapoor, et al. Plant Gene 19 (2019) 100182

functions in various pathological and physiological processes by acti-

vating secondary messengers or inducing gene transcription mechanism
which includes biotic and abiotic stress, cell wall lignifications, senes-
cence and root organogenesis (Nasir Khan et al., 2014).

6. ROS and RNS signalling in plants under various stresses

ROS plays a significant role in the form of signalling molecule which

acts in response to environmental stress in plants (Wilson et al., 2008;
del Río, 2013; Corpas et al., 2013a; Nasir Khan et al., 2014). Likewise,
nitrous oxide serves as a mediator, which works in coordination with
ROS as a defense response to plant pathogens (Bellin et al., 2013; Trapet
et al., 2015). Generally, it has been found that when plants are in
ecological or abiotic stress it leads to overproduction of RNS and ROS
(del Río and Puppo, 2009; Mittler et al., 2011; Airaki et al., 2012;
Sandalio et al., 2012; del Río, 2013; Baxter et al., 2013). Recurrent
synthesis of NO and ROS hinders the normally programmed cell death
(PCD). In this course, ROS and NO play a vital role. PCD is involved in
the various mechanism like growth and development along with it also Fig. 1. Pathway showing scavenging of reactive oxygen species (ROS) by an-
aid in eliminating the affected and impaired cells in response to pa- tioxidative defence system of plants (Adapted from Mittler, 2002).
thogen attack and environmental stresses (Wang et al., 2013a, b). It has
been documented that in the presence of O2, NO reacts with GSH
they cannot be completely ameliorated.
(glutathione), via S-nitrosylation reaction, which forms GSNO (S-ni-
Antioxidative defense system including both enzymatic antioxidants
troglutathione), an important reservoir of NO bioactivity mainly seen in
like superoxide dismutase (SOD), catalase (CAT), guaiacol peroxidase
different plant species (Ortega-Galisteo et al., 2012; Corpas and
(GPX), ascorbate peroxidase (APX), monodehydroascorbate reductase
Barroso, 2013; Corpas et al., 2013b, c; Xu et al., 2013; Kubienová et al.,
(MDHAR), dehydroascorbate reductase (DHAR), and glutathione re-
2014). Whereas, The RNS peroxynitrite (ONOO–), a nitrating/oxidant
ductase (GR) and non-enzymatic antioxidants such as ascorbate (AsA),
species which is synthesized by robust reaction between NO and O2
glutathione (GSH), carotenoids, tocopherols, and phenolics play major
(Radi, 2012; Trapet et al., 2015) and it is most commonly found in the
role for the amelioration of these ROS from the cells (Beckman and
organelles like peroxisomes (Xu et al., 2013; Corpas et al., 2013c;
Koppenol, 1996) (Figs. 1 and 2). Enhanced activities of these anti-
Corpas and Barroso, 2013). In the presence of NO and GSNO in plant
oxidative enzymes have been reported by many scientists that lead to
tissue, the formation of ONOO- leads to PTMs (Post-translational
the detoxification of ROS and reduction of oxidative damage in many
modification) in plants under both stress and normal conditions like
plants. The enhanced antioxidant potential is directly proportional to
protein nitration and S-nitrosylation (Corpas et al., 2013a; Romero-
the detoxification of free radicals and providing protection against the
Puertas et al., 2013; Kubienová et al., 2014). In peroxisomes, S-ni-
oxidative burst (Young and Woodside, 2001; Pacher et al., 2007; Flora,
trosylation inhibits the functioning of glycolate oxidase, catalase, and it
2009). The alternative way is to develop transgenic crops that might be
has been proposed that it can regulate the signalling molecule like H2O2
stress tolerant (Finkel and Holbrook, 2000; Uchida, 2003; Flora, 2009).
at the cellular level (Ortega-Galisteo et al., 2012). Whereas, the gen-
erated ONOO- molecule synthesize tyrosine nitration and cause a ni-
trosative alteration in plants, moreover, basal endogenous nitration 7. Regulation of ROS/RNS by antioxidant mechanism
may have a regulatory function. Recent studies conducted on pea plants
on EM-immunogold labelling revealed the presence of nitrated proteins Superoxide ion, hydrogen peroxide, hydroxyl radicals are the most
in the different compartment (sub-cellular level) of leaf cells, addition common ROS. At ground state, O2 is not harmful, but it becomes
to chloroplast, cytosol, mitochondria and peroxisomes (Ortega-Galisteo paramagnetic with two unpaired electrons with parallel spin after
et al., 2012; Barroso et al., 2013;). In addition to that, evaluation
through proteomic of isolated pea-leaf peroxisomes showed the emer-
gence of peroxisomal NADH-dependent hydroxypyruvate reductase
which is target enzyme for nitration and the reaction by peroxynitrite
leading to dysfunction of the enzyme (Corpas et al., 2013b; del Río,
2013).

6.1. Antioxidative defense system

During environmental stresses, the generation of ROS is enhanced,

consequently cause lipid peroxidation, inhibition of enzyme activities,
oxidation of proteins, deterioration of nucleic acids and leads to pro-
grammed cell death (PCD), hence cause damage to cells and finally
death (Masters, 1996; Tsao et al., 1998; Valko et al., 2006). On the
other hand, ROS have been considered as second messengers in a
number of cellular processes that also involve tolerance to environ-
mental stress tolerance (Ghafourifar and Chiueh, 1999; Bergendi et al.,
1999; Ghafourifar and Cadenas, 2005). Since ROS may prove damaging
or signalling molecule and it is directly related to maintaining the
balance between the generation and scavenging of ROS. ROS play
various roles in cells, so their level in the cells should be regulated to Fig. 2. Defensive responses of plants against various physiological stressors
avoid the injuries caused due to oxidative burst and at the same time, (Vickers et al., 2009)

4
D. Kapoor, et al.
absorbing a large amount of energy and it reacts with organic molecules
(Cracowski et al., 2002). Initially in the reaction 1O2 is formed and then
O2 is consecutively reduced to O2•−, H2O2, and •OH. In the biradical
form of oxygen, electrons have parallel spin. When sufficient energy is
absorbed, the spin of the unpaired electrlons reverses that form singlet
state of two electrons with opposite spin.
During light conditions, triplet chlorophyll (Chl) formation in the
antenna system and in the reaction centre of photosystem II triggers the
formation of highly reactive 1O2 (Montuschi et al., 2004). Inadequate
energy dissipation at the time of photosynthesis and charge re-
combination of the light-induced charge pair gives rise to the formation
of chlorophyll in triplet state in the antenna and reaction centre re-
spectively (Cracowski et al., 2002). The reaction of triplet state chlor-
ophyll with 3O2 forms the highly disparaging ROS 1O2:
Chl light 3Chl (1)
3Chl + 3O2 Chl + 1O2 (2)
1 7.1. Genes involved in the regulation of ROS
O2 formation occurs at the time of different abiotic stress condi-
tions like drought stress, salt stress and heavy metal stress etc. under the
inadequate supply of CO2, that leads to stomatal closure. 1O2, the
mainly the significant species liable for light-induced loss of photo-
system II (PSII) activity and cause cell death, leads to direct oxidation of
protein, unsaturated fatty acids, and DNA (Wilson et al., 2002) and by
reacting with deoxyguanosine causes amendment of nucleic acid
(Krieger-Liszkay et al., 2008). α-tocopherol, β-carotene after reacting
with D1 protein of photosystem II scavenge the 1O2. At the time of H2O2
production molecular O2 gains, one electron at a time and therefore
during reduction of O2, stable intermediates are formed in the step-wise
manner (Morrow, 2005). O2 •− is the primary ROS and in the cascade
of reactions, they give rise to the formation of secondary which can be
stimulated by enzymes or metals (Moret-Tatay et al., 2016). Types of
catalysts depend upon the type of cell or cell compartment. O2•− is a
moderately reactive, short-lived ROS and a nucleophilic reactant
having both oxidizing and reducing properties (Poli et al., 2004).
O2•− gains one electron and two protons to form H2O2 and then
superoxide dismutase enzyme cause dismutation of superoxide ion into
hydrogen peroxide with the release of molecular oxygen:
2O2• + 2H+ H2 O2 + O2 (3)
2O2• + 2H+ SOD H2 O2 + O2 (4)
Hydrogen peroxide is produced in the cells under normal as well as
various biotic and abiotic stress conditions such as drought, heavy
metals, salinity stress and attack of pathogens etc in the electron
transport chain of the cell organelles like plasma membrane, mi-
tochondria, chloroplast and endoplasmic reticulum (Flora, 2009).
Photooxidation reactions and β-oxidation of fatty acid are major
sources for the production of H2O2 in plant cells, which are further
required as a substrate for biosynthesis, for example in lignification and
suberization. It has no unpaired electrons, and can readily cross bio-
logical membranes and therefore cause oxidative damage.
H2O2 is the only ROS that can diffuse through aquaporins in the
membranes and over larger distances within the cell (Klaunig et al.,
2010) and is somewhat stable in comparison to other ROS. It is majorly
involved in regulating biological processes and provides tolerance
against different biotic and abiotic stress conditions even at low con-
centration (Bergendi et al., 1999; Pavlović et al., 2000). It can oxidize
cysteine (–SH) or methionine residues (–SCH3), and deactivate enzyme
activities by oxidizing their thiol groups, such as enzymes of Calvin
cycle, Cu/Zn-SOD, and Fe-SOD at their high concentration (Prasad,
2016). 50% of the activities of enzymes like phosphoribulokinase,
fructose-1,6-bisphosphatase, sedoheptulose-1,7-bisphosphatase has
been deteriorating by the accumulation of H2O2. It also oxidizes protein
kinases, phosphatases, and transcription factors containing thiolate
residues. It induces programmed cell death at high concentrations
(Pang et al., 2015). Both reactive oxygen species, O2•− and H2O2 are
5
Plant Gene 19 (2019) 100182
only more or less reactive. The cellular damage occurs when these two
radicals may get transformed into other more harmful reactive species.
•OH is also produced by both O2•− and H2O2 through Haber-Weiss
reaction and CAT and SOD enzymes are responsible for the removal of
these reactive species.
The Haber-Weiss reaction generates •OH from H2O2 and O2•−. It
consists of the following two reactions:
Fe3 + + O2 • Fe2 + + O2 (5)
First, Fe(III) is reduced by O2•−, followed by oxidation by dihy-
drogen peroxide (Fenton reaction)
Fe2 + + H2 O2 Fe3 + + OH + •OH (6)
and reaction:
O2• + H2 O2 •OH + OH + O2 (7)
Histidine kinase and DREB2A transcription factor are the two major
genes which are involved in the regulation of ROS via osmotic stress
signalling. It is also reported that MAPK AtMPK6 gene in Arabidopsis is
activated by osmotic stress and low temperature during oxidative stress
(Sharma et al., 2012). Borsani and his colleagues (Borsani et al., 2001)
studied that the increase in osmotic stress tolerance of transgenic Ara-
bidopsis expresses salicylate hydroxylase (NahG) gene, which might
result from decreased SA-mediated ROS generation. Some studies also
suggested that the Halliwell-Asada cycle is up-regulated by different
gene encoding enzymes such as APX, DHAR and MDHAR. The si-
multaneous expression of APX and Cu/Zn-SOD in the chloroplast of
tobacco enhances tolerance to various stresses (methyl viologen) (Kwon
et al., 2002). The overexpression of genes such as CAT and SOD in the
cytosol, APX and SOD in chloroplast and GR and SOD in cytosol also
enhances tolerance to various environmental stresses (Gill and Tuteja,
2010).
Arabidopsis genome contains Ten RBOH (respiratory burst oxidase
homolog) genes which encode plasma membrane-localized proteins
whereas, in the apoplast, apoplastic oxidase domain accounts for the
generation of superoxidase. The N-terminal extension in the cytoplasm
contains the phosphorylation domains and regulatory regions calcium-
binding EF-hands. Regulation of a respiratory burst oxidase homolog at
the plasma membrane by phosphorylation, calcium, nitric oxide avail-
ability is exposed to produces ROS signalling at apoplast (Gilroy et al.,
2016) which moves to the cytoplasm via aquaporins (Tian et al., 2016)
and further to mitochondria, peroxisomes and chloroplast which
changes the redox potential of TFs affecting gene expression (Takagi
et al., 2016; Huang et al., 2016a, b; Dietz et al., 2016a, b). Under stress
conditions, mitochondria, peroxisomes, and chloroplast extend their
membrane structure and change the status of ROS in the nuclei (Noctor
and Foyer, 2016). The ROS generating system is an essential aspect in
the subcellular sites in the adjustment process for the thiol redox net-
work. These networks are highly discussed in the literature. Although,
the drawback exists in their understanding related to the ROS-sensitive
switches involving their regulating mechanism of electron donor and an
electron acceptor. These could be ROS by their immediate reaction or
Redox-sensitive mediator. These are considered a part of sensitive tar-
gets for peroxidase and peroxiredoxins. Redox transmitters like thior-
edoxins are oxidized by peroxiredoxin, which results in the oxidation of
target protein. Apart from this, they act as a proximity-based oxidase
and redox-dependent interaction partner (Dietz et al., 2016a, b). The
dynamic and early modification of redox potential dissection happens
by undertaking certain steps which involve high sensitivity, untargeted
or targeted protein, mass spectrometry in association with blocking and
labelling. Various genes along with their localization and scavenging
network expressing ROS activity in Arabidopsis has been presented in
Table 1.
D. Kapoor, et al. Plant Gene 19 (2019) 100182

Table 1
List of genes, their localization and scavenging network of Arabidopsis expressing reactive oxygen species (ROS)
SL No. Genes Localization References

1 1-Cys Prxr Nuclei Horling et al. (2003)

2 2-Cys Prxr A Chloroplast Pulido et al. (2010)
3 2-Cys Prxr B Chloroplast Pulido et al. (2010)
4 2-Cys Prxr F Mitochondria Huang et al. (2016a, b)
5 Acyltransferase - Sui et al. (2017)
6 AOX Putative Mitochondria Tripathy and Oelmüller (2012)
7 AOX1A Mitochondria Nie et al. (2015)
8 AOX1B Mitochondria Umbach et al. (2005)
9 AOX1C Mitochondria Umbach et al. (2005)
10 AOX2 Mitochondria Umbach et al. (2005)
11 APX1 Cytosol Davletova et al. (2005)
12 APX2 Cytosol Suzuki et al. (2012a)
13 APX3 Peroxisomes/Chloroplast Tiew et al. (2015)
14 APX4 Chloroplast Koussevitzky et al. (2008)
15 APX5 Peroxisomes Koussevitzky et al. (2008)
16 APX6 Cytosol/Chloroplast/Mitochondria Koussevitzky et al. (2008)
17 APX7 Mitochondria Koussevitzky et al., (2008)
18 Blue Copper oxisomes Binding Protein - Desikan et al. (2001)
19 Blue Copperoxisomes Protein, Putative - Desikan et al. (2001)
20 Blue Copperoxisomes-Binding Protein III - Ihsan et al. (2017)
21 Blue Copperoxisomes-Binding Protein, 15K (Lamin) - Ihsan et al. (2017)
22 Cat1 Peroxisomes Del Río and López-Huertas (2016)
23 Cat2 Peroxisomes Del Río and López-Huertas (2016)
24 Cat3 Peroxisomes Del Río and López-Huertas (2016)
25 Copperoxisomes Binding - Like Protein Mitochondria Kaur et al. (2009)
26 Copperoxisomes-Binding Protein CUTA Chloroplast/Mitochondria Jaipargas et al. (2016)
27 Copperoxisomes-Binding Protein-Like Sec/Mitochondria Yang et al. (2014)
28 Cu/Znsod (CSD1) Cytosol Pilon et al. (2011)
29 Cu/Znsod (CSD2) Chloroplast Pilon et al. (2011)
30 Cu/Znsod (CSD3) Peroxisomes Holzmeister et al. (2014)
31 DHAR1 Chloroplast/Mitochondria Noshi et al. (2017)
32 DHAR2 Cytosol Noshi et al. (2017)
33 DHAR3 Cytosol/Chloroplast Waszczak et al. (2014)
34 DHAR4 Cytosol/Chloroplast Waszczak et al. (2014)
35 DHAR5 Cytosol/Chloroplast Waszczak et al. (2014)
36 Ferredoxin-Thioredoxin Reductase Chloroplast Wang et al. (2014)
37 Ferric Reductase (NADPH Oxidase) Membrane Sagi and Fluhr (2006)
38 Ferric-Chelate Reductase - Wu et al. (2005)
39 Ferritin 1 Chloroplast Bournier et al. (2013)
40 Ferritin 2 Chloroplast/Mitochondria Reyt et al. (2014)
41 Ferritin 3 Chloroplast/Mitochondria Reyt et al. (2014)
42 Ferritin 4 Chloroplast Reyt et al. (2014)
43 Fesod (FSD1) Chloroplast Myouga et al. (2008)
44 Fesod (FSD2) Chloroplast Myouga et al. (2008)
45 Fesod (FSD3) Chloroplast Myouga et al. (2008)
46 GPX1 Chloroplast Chang et al. (2009)
47 GPX2 Cytosol/Chloroplast Xu and Møller (2010)
48 GPX3 Mitochondria He et al. (2012)
49 GPX4 Cytosol Gaber (2014)
50 GPX5 Endoplasmic Reticulum Pérez-Martín et al. (2014)
51 GPX7 Chloroplast Chang et al. (2009)
52 GPX8 Cytosol/Chloroplast Gaber et al. (2012)
53 GR1 Cytosol Kataya and Reumann (2010)
54 GR2 Chloroplast/Mitochondria Ding et al. (2016)
55 Immutans Chloroplast Pogorelko et al. (2016)
56 MDAR1 Chloroplast/Mitochondria Suzuki et al. (2012b)
57 MDAR2 Cytosol Ramel et al. (2009)
58 MDAR3 Cytosol/Mitochondria Sewelam et al. (2013)
59 MDAR4 Cytosol Para et al. (2016)
60 MDAR5 Cytosol Ramel et al. (2009)
61 Mnsod (MSD1) Mitochondria Huang et al. (2016a, b)
62 Mnsod-Like - Sharma et al. (2012)
63 NADH-Ubiquinone Oxidoreductase - Kühn et al. (2015)
64 NADPH Oxidase (Rboha) Membrane Jiménez-Quesada et al. (2016)
65 NADPH Oxidase (Rbohb) Membrane Asai et al. (2008)
66 NADPH Oxidase (Rbohc) Membrane Krieger et al. (2016)
67 NADPH Oxidase (Rbohd) Membrane Kadota et al. (2015)
68 NADPH Oxidase (Rbohe) Membrane Jiménez-Quesada et al. (2016)
69 NADPH Oxidase (Rbohf) Membrane Kadota et al. (2015)
70 NADPH Oxidase (Rbohg) Membrane Orman-Ligeza et al. (2016)
71 NADPH Oxidase (Rbohh) Membrane Orman-Ligeza et al. (2016)
72 NADPH Oxidase (Rbohi) Membrane Orman-Ligeza et al. (2016)
73 NADPH Oxidase (Rbohj) Membrane Orman-Ligeza et al. (2016)
74 Phosphoadenylyl-Sulfate Reductase Chloroplast Mehterov et al. (2012)
(continued on next page)

6
D. Kapoor, et al. Plant Gene 19 (2019) 100182

Table 1 (continued)

SL No. Genes Localization References

75 Phospholipid GPX6 Chloroplast/Mitochondria Milla et al. (2003)

76 Prxr Q Chloroplast Porat et al. (2011)
77 Putative Blue Copperoxisomes-Binding Protein Mitochondria Desikan et al. (2001)
78 Putative NADPH Oxidase Membrane/Mitochondria Tripathy and Oelmüller (2012)
79 Flavocytochrome Sec/Chloroplast Andronis et al. (2014)
80 Stromal-APX Chloroplast/Mitochondria Davletova et al. (2005)
81 Thioredoxin Family Mitochondria Nikkanen et al. (2017)
82 Thioredoxin Family Chloroplast Zhang et al. (2018)
83 Thioredoxin Family Endoplasmic Reticulum/Mitochondria Chaube and Werstuck (2016)
84 Thioredoxin Family Cytosol/Mitochondria Cha et al. (2015)
85 Thioredoxin Family Cytosol Cha et al. (2015)
86 Thioredoxin Family Chloroplast/Mitochondria Cha et al. (2015)
87 Thioredoxin H -Related Cytosol/Mitochondria Dietz et al. (2016a, b)
88 Thioredoxin H-Type 1 (TRX-H-1) Cytosol Zhang et al. (2011)
89 Thioredoxin H-Type 2 Cytosol Shahpiri et al. (2009)
90 Thioredoxin H-Type 3 Cytosol Shahpiri et al. (2009)
91 Thioredoxin H-Type 4 (TRX-H-4) Cytosol Shahpiri et al. (2009)
92 Thioredoxin H-Type 5 (TRX-H-5) Cytosol Park et al. (2017)
93 Thioredoxin M-Type 1 (TRX-M1) Chloroplast/Mitochondria Cheng et al. (2014)
94 Thioredoxin M-Type 2 Chloroplast Wang et al. (2013a, b)
95 Thioredoxin M-Type 3 Chloroplast Laloi et al. (2004)
96 Thioredoxin M-Type 4 Chloroplast Wang et al. (2013a, b)
97 Thioredoxin Reductase 1 Cytosol Serrato et al. (2013)
98 Thioredoxin Reductase 2 Cytosol/Mitochondria Lopert et al. (2012)
99 Thioredoxin Reductase, Putative Chloroplast Lepistö et al. (2009)
100 Thioredoxin X Chloroplast/Mitochondria Lepistö et al., 2009
101 Thylakoid-APX Chloroplast Asada (2006)
102 Type 2 Prxr A Membrane/Chloroplast Mittler et al. (2004)
103 Type 2 Prxr B Cytosol Li et al. (2012)
104 Type 2 Prxr C Cytosol Li et al. (2012)
105 Type 2 Prxr D Cytosol Li et al. (2012)
106 Type 2 Prxr E Chloroplast/Mitochondria Mittler et al. (2004)
107 Type 2 Prxr -Related Cytosol Li et al. (2017)

7.2. Gene level/transcription factor regulation of Oxidative/Nitrosative
stress
Instability between reactive oxygen species (ROS) and antioxidants
result in oxidative stress which occurs either of accumulation of ROS or
diminution of antioxidants (Schieber and Chandel, 2014). In stress
conditions, cells attempt to stabilize the effect of oxidants and restore
the redox balance by silencing or gene activation, structural proteins
and transcription factors (Sosa et al., 2013). The correlation between
reduced and oxidized glutathione is one of the utmost factors in de-
termining the stress in the body. ROS is subjected to change in the
structure of DNA, triggering of various stresses induced transcription
factors, modification of lipids and proteins, and production of anti-in-
flammatory and pro-inflammatory cytokines (Gu et al., 2013). Oxida-
tive stress lead to various DNA modifications which incriminate de-
gradation of purine, pyrimidine, translocations, deletions, cross-
linkages, mutations etc. (Cadet and Davies, 2017). These modifications
often lead to various autoimmune, cardiovascular, neurodegenerative,
ageing and carcinogenesis diseases (Bhat et al., 2015). Non-redox me-
tals such as Fe, Cd, Cr and Ar are mostly involved in causing carcino-
genesis via ROS (Lee et al., 2012). Binding of ROS with thiol groups of
DNA and generation of free radicals during oxidative stress results in
ageing and neurodegenerative disorders (Bhat et al., 2015; Gu et al.,
2013). DNA damage results in the formation of 8-OH-G which is a
known potent biomarker for carcinogenesis (Grigorov, 2012). GC rich
sequences are always susceptible to oxidant attacks which results in the
formation 8-OH-G which modifies binding sites of transcription factors
and changes the expression of Sp1 and AP1 target sequences. In addi-
tion to that 8, 5′-cyclo-2′-deoxyadenosine (cyclo-dA) impairs the
binding of TATA-binding protein by altering the DNA structure
(Zaliznyak et al., 2012). Instability of microsatellite regions in DNA is
influenced by hydroxyl radicals and redox active metal ions (Chervona
and Costa, 2012). Gene silencing is induced by methylation at CpG sites
in DNA via the epigenetic mechanism in which 5-MeCyt to 5-hydro-
xymethyl uracil (5-OHMeUra) is oxidized by deamination reactions of
5-hydroxymethyl cytosine or thymine intermediates (Birben et al.,
2012). In addition to that oxidative stress also lead to cause irregula-
rities in chromatin organization and DNA repair activity (Wright et al.,
2014). ROS disrupts the lipid bilayer membrane and induces lipid
peroxidation that inactivates receptors of membrane-bound proteins
and escalated tissue permeability (Biney et al., 2018). Unsaturated al-
dehydes and MDA inactivates various cellular proteins by producing
cross-linkage proteins (Ayala et al., 2014). Other products of lipid
peroxidases such as thiobarbituric acid & isoprostanes trigger oxidative
stress by behaving as indirect biomarkers by depleting intracellular
GSH (Souse et al., 2012). Changes in isoelectric charges of proteins,
oxidation of particular amino acids, and fragmentation of peptide chain
etc. all these factors were highly influenced by oxidative stress which
leads to susceptibility to proteolysis by disrupting them by specific
proteases (Anjum et al., 2015). Methionine and cysteine proteins are
vulnerable to oxidation which causes protein unfolding, degradation
and conformational changes in its structure (Wang et al., 2012a, b). By
this, proteins such as methionine are converted to methionine sulfoxide,
sulfhydryl groups to form disulfide bridges, phenylalanine to o-tyrosine
and carboxyl or carbonyl functional groups is attached to the various
side chains of functional groups by oxidative reaction mechanism re-
sulting in the fragmentation of its structure (Bartosz and Sadowska-
Bartosz, 2015). ROS can persuade the expression of various genes
which are involved in signal transduction (Wrzaczek et al., 2013). Al-
though, GSH and GSSH ratio plays a vital role in protecting the cell
from various oxidative stress (Zitka et al., 2012). Changes in this ratio
activate certain redox transcription factors such as hypoxia-inducible
factor 1, nuclear factor of activated T cells, AP-1 and NF-κB which are
tangled in the inflammatory response (Kaur et al., 2015).
Triggering of translation factors by means of ROS is accomplished
by signal transduction that transmits the information from outside to

7
D. Kapoor, et al.
within cell (Kreslavski et al., 2012). The targets of ROS in translation
factors includes changes in threonine/serine kinases, protein tyrosine
phosphatases, receptor for the vascular endothelial growth factor, tyr-
osine kinase receptors which change the mechanism of cell differ-
entiation, cell proliferation and finally apoptosis (Ray et al., 2012).
During oxidative stress, most of the cysteine residues (AP-1 subunits,
inhibitory κ-B kinase and c-Jun) undergoes reversible S-glutathionyla-
tion (Farooqui, 2014). TRX and Glutaredoxin have also been docu-
mented to play a vital role in the regulation of signaling pathways
(redox-sensitive) such as JNK, p38 mitogen-activated protein kinase,
AP-1 and NF-κB (Truong and Carroll, 2012). A number of kinases have
also been documented which phosphorylate IκBs at the major sites of
the serine residues which are the main targets of oxidative stress for
activation of NF-κB reducing agents (Kanarek and Ben-Neriah, 2012). It
enhances the binding of NF-κB DNA while oxidative agents inhibit it.
TRX blocks IκB by inhibiting activation of NF-κB but helps in the
binding of NF-κB DNA in the nucleus (Kelleher et al., 2014). This results
in the stimulation of various anti-oxidant related genes which regulates
differentiation, proliferation angiogenesis of cells and regulates gene
expression which anticipates to immune-response factors (IL1β, IL-8,
tumour necrosis factor-α, IL-6 and other adhesion molecules (Lee and
Yang, 2012). Some redox metals induce the activation and generation
of AP-1 which imbalance GSH/GSSG ratio and prevents AP1 binding
with DNA (Mikhed et al., 2015). Reduction in the cysteine molecules in
the domain of DNA binding increases the DNA binding with Fos/Jun
heterodimer whereas, the formation of disulphide bridges inhibits
binding of DNA with AP-1 (Kelley et al., 2012).
ROS are inevitable by-products of regular cell metabolism. It is
generated by electron transport activities of the plasma membrane,
mitochondria, and chloroplast or as a byproduct of several metabolic
pathways restricted in different compartments of cells. Under standard
growth conditions, stress production in various compartments of cells is
very low. Conversely, various environmental stresses such as UV-B,
salinity, chilling drought, and metal toxicity, if sustained over to a
certain extent, disturb the cellular homeostasis and boost the produc-
tion of ROS. ROS play two major roles in plants; in small amounts, they
act as signalling molecules that arbitrate various plant responses in
plant cells under stresses, while in high concentrations they cause ag-
gravating damage to various cellular components. The heightened level
of ROS causes oxidative damage to DNA, protein and lipid leading to
altered intrinsic membrane properties like DNA damage, inhibition of
protein synthesis, protein crosslinking, loss of enzyme activity, fluidity,
ion transport ultimately resulting in apoptosis. In order to evade the
oxidative damage, most of the higher plants have a complex anti-oxi-
dative defense system comprising of enzymatic and non-enzymatic
components. Although rapid progress in recombinant DNA technology
in recent years, there are many qualms and gaps in our information of
ROS formation and their negative effect on plants mainly due to the
high reactivity of ROS and short half-life. Future studies on the for-
mation and environmental fate of ROS using advanced recombinant
DNA technology will assist in developing a wider view of the role of
ROS in plants. Future progress in metabolomics, proteomics and
genomics will help in the lucid understanding of various biochemical
networks involved in various cellular responses to oxidative stress.
Improved understanding of these will be helpful in producing plants
with an in-built capacity of enhanced levels of tolerance to ROS using
biotechnological approach.
8. Conclusions and future perspectives
This study is important in the present scenario as our plants are
facing different types of stress conditions that lead to the production of
reactive oxygen and nitrogen species. In recent years, deteriorative ef-
fects of ROS/RNS and mechanism illustrating the roles of antioxidants
to ameliorate these free radicals have become the major issue for the
scientists. These free radicals cannot be avoided as they also act as by-
8
Plant Gene 19 (2019) 100182
products of normal cell metabolism. Extreme environmental conditions
like drought, salinity, chilling, metal toxicity and UV-B disrupt the
cellular homeostasis and enhance the production of ROS. ROS play two
different roles in plants; at low concentrations, they act as signalling
molecules and mediate various plant responses in plant cells that in-
clude responses under stresses, whereas at high concentrations they are
hazardous to cellular components. To combat the oxidative damage
caused by free radicals, plants possess a multifaceted antioxidative
defense system which consists of non-enzymatic and enzymatic com-
ponents. Antioxidants demonstrate pro-oxidant activity depending on
the specific conditions that particularly depends upon their dosage and
redox conditions in the cell. Moreover, antioxidants may have reduced
free-radical damage to normal tissues that triggers reduced toxicity.
Supplementation of antioxidants does not influence the cytotoxic me-
chanisms of the drugs. Hence it can be concluded that enzymatic and
non-enzymatic antioxidants play significant roles in the amelioration of
oxidants, which are responsible for the oxidative burst. This study will
help in understanding the physiology of plants when exposed to stress
and the ameliorative mechanisms activated inside plant cells. Defensive
system of plants helps in the normal functioning of plant cells even
under the stress conditions. By understanding the basic mechanism
behind this, plant breeders also can produce such improved varieties
that can tolerate/resist the stress.
Conflicts of interest
Authors declare that no conflicts of interest exist.
Compliance with ethical requirements
This article does not contain any studies with animals performed by
any of the authors.
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