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Biology and Biotechnology of Environmental Stress Tolerance in Plants, Volume 3

domain-containing protein 47, glycine-rich protein, and rRNA processing

protein (Rrp5) (Yin & Komatsu, 2015). The nuclear fraction of soybean root

tip at the initial stage of flooding stress was analyzed by Yin & Komatsu

(2016). A total of 365 nuclear proteins were altered in flooding stress.

After flooding, the nuclear proteome of soybean revealed different H2A

isoforms as well as decreased H1 and H3, indicating extensive chromatin

remodeling. Furthermore, in flooded soybean, four exon-junction complex-

related proteins including NOP1/NOP56, which operate upstream of 60S

pre-ribosome biogenesis, were reduced.

13.3.2 MITOCHONDRIA

Mitochondrial proteome study has a new insight into understanding the

stress response of plants during abiotic stress factors. Mitochondria is the

cell’s powerhouse, responsible for nucleotide and vitamin synthesis, lipid,

and amino acid metabolism, and the photorespiratory pathway (Miller et al.,

2005; Liu et al., 2019). Under stress, the mitochondrial proteome showed

an increased level of ROS scavenging enzyme (Mn-SOD) in pea and wheat

(Taylor et al., 2005; Jacoby et al., 2010). For a complete examination of mito­

chondrial activities in plants, an Arabidopsis mitochondrial proteome project

was launched. The first 2-DE-PAGE analysis of mitochondrial protein was

performed by Kruft et al. (2001). After that, separating proteins for studying

the plant mitochondrial proteome under stressful conditions received a lot of

interest. They identified 52 protein spots that are collaborating with various

processes, such as the citric acid cycle, nucleotide, and amino acid metabo­

lism, respiration, protein biosynthesis, and mitochondrial assembly.

Mitochondria are crucial in cell survival and are a critical location of

oxidative stress and cellular response. Common stressors like drought, cold,

and herbicides were used to study the reaction of mitochondria in Pisum

sativum plants. To varying degrees, all of these treatments altered the photo­

synthetic and respiratory rates of pea leaves, but only herbicides increased

lipid peroxidation buildup (Taylor et al., 2005). Mitochondria isolated from

stressed pea plants retained their electron transport chain function, but the

number of uncoupling proteins, non-phosphorylating respiratory pathways,

and oxidative modification of lipoic acid moieties on mitochondrial proteins

all changed. The degradation of important matrix enzymes is different under

freezing and drought stressors, according to 2D-PAGE and MS analyses of

soluble proteins from mitochondria. Furthermore, variable activation of heat