Recent Insights into the Physio-Biochemical and Molecular Mechanisms of Low Temperature Stress in Tomato
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Climate change has emerged as a crucial global issue that significantly threatens the survival of plants. In particular, low temperature (LT) is one of the critical environmental factors that influence plant morphological, physiological, and biochemical changes during both the vegetative and reproductive growth stages. LT, including abrupt drops in temperature, as well as winter conditions, can cause detrimental effects on the growth and development of tomato plants, ranging from sowing, transplanting, truss appearance, flowering, fertilization, flowering, fruit ripening, and yields. Therefore, it is imperative to understand the comprehensive mechanisms underlying the adaptation and acclimation of tomato plants to LT, from the morphological changes to the molecular levels. In this review, we discuss the previous and current knowledge of morphological, physiological, and biochemical changes, which contain vegetative and reproductive parameters involving the leaf length (LL), plant height (PH) stem diameter (SD), fruit set (FS), fruit ripening (FS), and fruit yield (FY), as well as photosynthetic parameters, cell membrane stability, osmolytes, and ROS homeostasis via antioxidants scavenging systems during LT stress in tomato plants. Moreover, we highlight recent advances in the understanding of molecular mechanisms, including LT perception, signaling transduction, gene regulation, and fruit ripening and epigenetic regulation. The comprehensive understanding of LT response provides a solid basis to develop the LT-resistant varieties for sustainable tomato production under the ever-changing temperature fluctuations.Keywords:
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Plant Physiology
When measured at a same CO(2) concentration, net photosynthetic rate is often significantly lower in long-term high CO(2)-grown plants than the ambient CO(2)-grown ones. This phenomenon is termed photosynthetic acclimation or down-regulation. Although there have been many reports and reviews, the mechanism(s) of the photosynthetic acclimation is not very clear. Combining the work of the authors' group, this paper briefly reviews the progress in studies on the mechanism(s) of the photosynthetic acclimation to elevated CO(2). It is suggested that besides the possible effects of respiration enhancement and excessive photosynthate accumulation, RuBP carboxylation limitation and RuBP regeneration limitation are probably the main factors leading to the photosynthetic acclimation.
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Osmoregulation
Osmotic shock
Methylamines
Intracellular Fluid
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Cells respond to osmotic swelling by releasing inorganic ions and small organic molecules (organic osmolytes). In many cell-types, osmotic swelling results in the activation of an outwardly-rectifying anion-selective current. The channel underlying this current has a significant permeability to a number of organic osmolytes and may play a role in the hypoosmotically-activated efflux of these compounds. However, there is also evidence that the volume-regulatory efflux of organic osmolytes involves other pathways which may be selective for neutral osmolytes over anions.
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Efflux
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Osmolyte
Betaine
Methylamines
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With rising level of CO2 in the atmosphere plants are expected to be exposed to higher concentration of CO2. Since, CO2 is a substrate limiting photosynthesis particularly in C3 plants in the present atmosphere, the impact of elevated CO2 would depend mainly on how photosynthesis acclimates or adjusts to the long term elevated level of CO2. Photosynthetic acclimation is a change in photosynthetic efficiency of leaves due to long term exposure to elevated CO2. This change in photosynthetic efficiency could be a biochemical adjustment that may improve the overall performance of a plant in a high CO2 environment or it could be due to metabolic compulsions as a result of physiological dysfunction. Acclimation has generally become synonymous with the word response, if long term exposure to elevated CO2 decreases the photosynthesis rate (Pn) at a given CO2 level, it is called negative acclimation, if it stimulates Pn at a given CO2 level, it is called positive acclimation. Photosynthetic acclimation is clearly revealed by comparing Pn of ambient and elevated CO2 grown plants at same level of CO2. Species level differences in acclimation to elevated CO2 have been reported. The physiological basis of differential photosynthetic acclimation to elevated CO2 is discussed in relation to the regulation of photosynthesis and photosynthetic carbon partitioning at cellular level.
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Osmolytes are naturally occurring organic compounds, which represent different chemical classes including amino acids, methylamines, and polyols. By accumulating high concentrations of osmolytes, organisms adapt to perturbations that can cause structural changes in their cellular proteins. Osmolytes shift equilibrium toward natively-folded conformations by raising the free energy of the unfolded state. As osmolytes predominantly affect the protein backbone, the balance between osmolyte-backbone interactions and amino acid side chain-solvent interactions determines protein folding. Abnormal cell volume regulation significantly contributes to the pathophysiology of several disorders, and cells respond to these changes by importing, exporting, or synthesizing osmolytes to maintain volume homeostasis. In recent years, it has become quite evident that cells regulate many biological processes such as protein folding, protein disaggregation, and protein-protein interactions via accumulation of specific osmolytes. Many genetic diseases are attributed to the problems associated with protein misfolding/aggregation, and it has been shown that certain osmolytes can protect these proteins from misfolding. Thus, osmolytes can be utilized as therapeutic targets for such diseases. In this review article, we discuss the role of naturally occurring osmolytes in protein stability, underlying mechanisms, and their potential use as therapeutic molecules.
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Folding (DSP implementation)
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Mixed osmolytes: The degree to which one osmolyte affects the protein stabilizing ability of another
Mixtures of organic osmolytes occur in cells of many organisms, raising the question of whether their actions on protein stability are independent or synergistic. To investigate this question it is desirable to develop a system that permits evaluation of the effect of one osmolyte on the efficacy of another to either force-fold or denature a protein. A means of evaluating the efficacy of an osmolyte is provided by its m-value, an experimental quantity that measures the ability of the osmolyte to force a protein to unfold or fold. An experimental system is presented that enables evaluations of the m-values of osmolytes in the presence and absence of a second osmolyte. The experimental system involves use of a marginally stable protein in 10 mM buffer (pH 7, 200 mM salt, and 34 degrees C) that is at the midpoint of its native to denatured transition. These conditions enable determination of m-values for protecting and denaturing osmolytes in the presence and absence of a second osmolyte, permitting assessment of the extent to which the two osmolytes affect each other's efficacy. The two osmolytes investigated in this work are the denaturing osmolyte, urea, and the protecting osmolyte, sarcosine. Results show unequivocally that neither osmolyte alters the efficacy of the other in forcing the protein to fold or unfold-the osmolytes act independently on the protein despite their combined concentrations being in the multi-molar range. These osmolytes avoid altering one another's efficacy at these high concentrations because the number of osmolyte interaction sites on the protein is large and the binding constants are quite small. Consequently, the site occupancies are low enough in number that the two osmolytes neither compete nor cooperate in interacting with the protein.
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Protein Stability
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Folding (DSP implementation)
Protein Stability
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This chapter contains sections titled: Introduction Denaturing Osmolytes Protecting Osmolytes Mixed Osmolytes Conclusions Acknowledgments References
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Protein Stability
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Methylamines
Chemical chaperone
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