Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.1.2.13 (aldolase)
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Protein metabolism plays an important role in plant adaptation to heat stress. This study was designed to identify heat-responsive proteins in roots associated with thermotolerance for two C3 grass species contrasting in heat tolerance, thermal Agrostis scabra and heat-sensitive Agrostis stolonifera L. Plants were exposed to 20 degrees C (control), 30 C (moderate heat stress), or 40 degrees C (severe heat stress) in growth chambers. Roots were harvested at 2 d and 10 d after temperature treatment. Proteins were extracted and separated by two-dimensional polyacrylamide gel electrophoresis. Seventy protein spots were regulated by heat stress in at least one species. Under both moderate and severe heat stress, more proteins were down-regulated than were up-regulated, and thermal A. scabra roots had more up-regulated proteins than A. stolonifera roots. The sequences of 66 differentially expressed protein spots were identified using mass spectrometry. The results suggested that the up-regulation of sucrose synthase, glutathione S-transferase, superoxide dismutase, and heat shock protein Sti (stress-inducible protein) may contribute to the superior root thermotolerance of A. scabra. In addition, phosphoproteomic analysis indicated that two isoforms of fructose-biphosphate aldolase were highly phosphorylated under heat stress, and thermal A. scabra had greater phosphorylation than A. stolonifera, suggesting that the aldolase phosphorylation might be involved in root thermotolerance.
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PMID:Root proteomic responses to heat stress in two Agrostis grass species contrasting in heat tolerance. 1900 11

Knowledge of heat-responsive proteins is critical for further understanding of the molecular mechanisms of heat tolerance. The objective of this study was to compare proteins differentially expressed in two C(3) grass species contrasting in heat tolerance, heat-tolerant thermal Agrostis scabra and heat-sensitive Agrostis stolonifera L., and to identify heat-responsive proteins for short- and long-term responses. Plants were exposed to 20/15 degrees C (day/night, control) or 40/35 degrees C (day/night, heat stress) in growth chambers. Leaves were harvested at 2 and 10 days after temperature treatment. Proteins were extracted and separated by fluorescence difference gel electrophoresis (DIGE). Thermal A. scabra had superior heat tolerance than A. stolonifera, as indicated by the maintenance of higher chlorophyll content and photochemical efficiency under heat stress. The two-dimensional difference electrophoresis detected 68 heat-responsive proteins in the two species. Thermal A. scabra had more protein spots either down- or up-regulated at 2 days of heat stress, but fewer protein spots were altered at 10 days of heat stress compared with A. stolonifera. Many protein spots exhibited transient down-regulation in thermal A. scabra (only at 2 days of heat treatment), whereas down-regulation of many proteins was also found at 10 days of heat treatment in A. stolonifera, which suggested that protein metabolism in thermal A. scabra might acclimate to heat stress more rapidly than those in A. stolonifera. The sequences of 56 differentially expressed protein spots were identified using mass spectrometry. The results suggest that the maintenance or less severe down-regulation of proteins during long-term (10 days) heat stress may contribute to the superior heat tolerance in thermal A. scabra, including those involved in photosynthesis [RuBisCo, RuBisCo activase, chloroplastic glyceraldehydes-3-phosphate dehydrogenase (GAPDH), chloroplastic aldolase, oxygen-evolving complex, photosystem I subunits], dark respiration (cytosolic GAPDH, cytoplasmic aldolase, malate dehydrogenase, hydroxypyruvate reductase, sedoheptulose-1,7-bisphosphatase), photorespiration [(hydroxypyruvate reductase, alanine aminotransferase (AlaAT), hydroxymethyltransferase (SHMT), glycine decarboxylase (GDC)], as well as heat and oxidative stress protection [heat shock cognate (HSC) 70 and FtsH-like protein].
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PMID:Differential proteomic response to heat stress in thermal Agrostis scabra and heat-sensitive Agrostis stolonifera. 2011 35

Ozone (O3), a potent air pollutant and a significant greenhouse gas, has been recognized as a major component of global climate change. However, current increasing trends in its background level are projecting a more severe threat to natural and cultivated plants in the near future. The present study has been designed to evaluate the impact of elevated concentrations of O3 on phenotypical, physiological, and biochemical traits in two high-yielding cultivars of wheat, followed by analysis of the leaf proteome using one/two-dimensional gel electrophoresis (1-/2-DGE) coupled to immunoblotting and mass spectrometry analyses under near-natural conditions using open top chambers. Prominently, O3 exposure caused specific foliar injury in both the wheat cultivars. Results also showed that O3 stress significantly decreased photosynthetic rate, stomatal conductance, and chlorophyll fluorescence kinetics (Fv/Fm) in test cultivars. Biochemical evaluations further revealed a higher loss in photosynthetic pigments, whereas a significantly induced antioxidant system under elevated O3 concentrations pointed toward an ability of O3 to generate oxidative stress. 1-DGE analysis showed drastic reductions in the abundantly present ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) large and small subunits. Western blot analysis confirmed induced accumulation of antioxidative enzymes like superoxide dismutase and ascorbate peroxidase protein(s) and common defense/stress-related thaumatin-like protein(s). 2-DGE analysis revealed a total of 38 differentially expressed protein spots, common in both the wheat cultivars. Among those, some major leaf photosynthetic proteins (including RuBisCO and RuBisCO activase) and important energy metabolism proteins (including ATP synthase, aldolase, and phosphoglycerate kinase) were drastically reduced, whereas some stress/defense-related proteins (such as harpin-binding protein and germin-like protein) were induced. In all, the present study reveals an intimate molecular network provoked by O3 affecting photosynthesis and triggering antioxidative defense and stress-related proteins culminating in accelerated foliar injury in wheat plants.
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PMID:Investigating the impact of elevated levels of ozone on tropical wheat using integrated phenotypical, physiological, biochemical, and proteomics approaches. 2070 Dec 90