Plants regularly face adverse growth conditions, such as drought, salinity, chilling, freezing, and high temperatures. These stresses can delay growth and development, reduce productivity, and, in extreme cases, cause plant death. Plant stress responses are dynamic and involve complex cross-talk between different regulatory levels, including adjustment of metabolism and gene expression for physiological and morphological adaptation. In this review, information about metabolic regulation in response to drought, extreme temperature, and salinity stress is summarized and the signalling events involved in mediating stress-induced metabolic changes are presented.

Drought, salt, and temperature stress-induced metabolic rearrangements and regulatory networks

Halophytes are defined as plants that are adapted to live in soils containing high concentrations of salt and benefiting from it, and thus represent an ideal model to understand complex physiological and genetic mechanisms of salinity stress tolerance. It is also known that oxidative stress signalling and reactive oxygen species (ROS) detoxification are both essential components of salinity stress tolerance mechanisms. This paper comprehensively reviews the differences in ROS homeostasis between halophytes and glycophytes in an attempt to answer the questions of whether stress-induced ROS production is similar between halophytes and glycophytes; is the superior salinity tolerance in halophytes attributed to higher antioxidant activity; and is there something special about the specific ‘pool’ of enzymatic and non-enzymatic antioxidants in halophytes. We argue that truly salt-tolerant species possessing efficient mechanisms for Na + exclusion from the cytosol may not require a high level of antioxidant activity, as they simply do not allow excessive ROS production in the first instance. We also suggest that H 2O2 ‘signatures’ may operate in plant signalling networks, in addition to well-known cytosolic calcium ‘signatures’. According to the suggested concept, the intrinsically higher superoxide dismutase (SOD) levels in halophytes are required for rapid induction of the H2O2 ‘signature’, and to trigger a cascade of adaptive responses (both genetic and physiological), while the role of other enzymatic antioxidants may be in decreasing the basal levels of H2O2, once the signalling has been processed. Finally, we emphasize the importance of non-enzymatic antioxidants as the only effective means to prevent detrimental effects of hydroxyl radicals on cellular structures.

ROS homeostasis in halophytes in the context of salinity stress tolerance

Current research on inositols mainly focuses on myo-inositol (Ins) derivatives in eukaryotic cells, and in particular on the many roles of Ins phospholipids and polyphosphorylated Ins derivatives. However, inositols and their derivatives are more versatile than this--they have acquired diverse functions over the course of evolution. Given the central involvement of primordial bacteria and archaea in the emergence of eukaryotes, what is the status of inositol derivatives in these groups of organisms, and how might inositol, inositol lipids and inositol phosphates have become ubiquitous constituents of eukaryotes? And how, later, might the multifarious functions of inositol derivatives have emerged during eukaryote diversification?

Inositol derivatives: evolution and functions

Improving salinity tolerance of plants through conventional breeding and genetic engineering: An analytical comparison.

While H2O2 has been implicated in numerous plant environmental responses, normal levels and variabilities are poorly established, and estimates of leaf tissue concentrations span more than three orders of magnitude, even in a single species under similar conditions. Here, leaf tissue H2O2 contents under natural conditions are reported after determining (i) that H2O2 in extracts was stable with time, (ii) that H2O2 added to the extract was recovered quantitatively, and (iii) that the H2O2 calibration curve was unaffected (or quantifiably affected) by the extract. The broad applicability of the protocol and variability in leaf concentrations were demonstrated using tissue collected from several habitats in association with three, more extensive, experiments. The first involved nychthemeral studies of the mangrove, Rhizophora mangle L. Lowest H2O2 levels occurred in the early morning and near sunset, with higher levels both at midday and at night. Second, using five temperate species in Spring, concentrations were compared on a warm, sunny day and a cool, cloudy day. Higher concentrations were found on the warm day for Aesculus glabra Willd., Glechoma hederacea L., Plantago major L., and Viola soraria Willd., while there were no differences in Quercus macrocarpa Michx. Finally, the effects of elevated CO2 and ozone were examined in soybean, Glycine max L. Pioneer 93B15 under Free Air gas Concentration Enrichment (FACE) conditions. Both supplements led to elevated H2O2. Overall, mean leaf, midday, and mid-summer H2O2 concentrations ranged from 0.67 lmol (gFW) 21 in mangrove to 3.6 lmol (gFW) 21 in A. glabra Willd. Greatest within-species differences were only 2.5-fold in any of the studies.

/pdf/hydrogen-peroxide-concentrations-in-leaves-under-natural-1csszigp4j.pdf

Hydrogen peroxide concentrations in leaves under natural conditions

http://www.jbc.org/content/279/27/28539.full.pdf

A novel salt-tolerant L-myo-inositol-1-phosphate synthase from Porteresia coarctata (Roxb.) Tateoka, a halophytic wild rice: molecular cloning, bacterial overexpression, characterization, and functional introgression into tobacco-conferring salt tolerance phenotype.

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/S0014-5793%2803%2900974-8

Diversification and evolution of L‐myo‐inositol 1‐phosphate synthase

Synechocystis Fe superoxide dismutase gene confers oxidative stress tolerance to Escherichia coli.

https://link.springer.com/content/pdf/10.1007%2F0-387-27600-9_13.pdf

Evolutionary divergence of L-myo-inositol 1-phosphate synthase: significance of a "core catalytic structure".

l-myo-inositol 1-phosphate synthase (EC 5.5.1.4; MIPS) catalyzes the first rate limiting conversion of d-glucose 6-phosphate to l-myo-inositol 1-phosphate in the inositol biosynthetic pathway. In an earlier communication we have reported two forms of MIPS in Synechocystis sp. PCC6803 (Chatterjee et al. in Planta 218:989–998, 2004). One of the forms with a ~50 kDa subunit has been found to be coded by an as yet unassigned ORF, sll1722. In the present study we have purified the second isoform of MIPS as a ~65 kDa protein from the crude extract of Synechocystis sp. PCC6803 to apparent homogeneity and biochemically characterized. MALDI-TOF analysis of the 65 kDa protein led to its identification as acetolactate synthase large subunit (EC 2.2.1.6; ALS), the putatively assigned ORF sll1981 of Synechocystis sp. PCC6803. The PCR amplified ~1.6 kb product of sll1981 was found to functionally complement the yeast inositol auxotroph, FY250 and could be expressed as an immunoreactive ~65 kDa MIPS protein in the natural inositol auxotroph, Schizosaccharomyces pombe. In vitro MIPS activity and cross reactivity against MIPS antibody of purified recombinant sll1981 further consolidated its identity as the second probable MIPS gene in Synechocystis sp. PCC6803. Sequence comparison along with available crystal structure analysis of the yeast MIPS reveals conservation of several amino acids in sll1981 essential for substrate and co-factor binding. Comparison with other prokaryotic and eukaryotic MIPS sequences and phylogenetic analysis, however, revealed that like sll1722, sll1981 is quite divergent from others. It is probable that sll1981 may code for a bifunctional enzyme protein having conserved domains for both MIPS and acetolactate synthase (ALS) activities.

Anirban Chatterjee

Papers

A novel salt-tolerant L-myo-inositol-1-phosphate synthase from Porteresia coarctata (Roxb.) Tateoka, a halophytic wild rice: molecular cloning, bacterial overexpression, characterization, and functional introgression into tobacco-conferring salt tolerance phenotype.

Diversification and evolution of L‐myo‐inositol 1‐phosphate synthase

Synechocystis Fe superoxide dismutase gene confers oxidative stress tolerance to Escherichia coli.

Evolutionary divergence of L-myo-inositol 1-phosphate synthase: significance of a "core catalytic structure".

sll1981, an acetolactate synthase homologue of Synechocystis sp. PCC6803, functions as l-myo-inositol 1-phosphate synthase