How potassium affect protein synthesis on plant? | …

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On the role of intracellular potassium in protein synthesis

Potassium (Potash) Protein synthesis, favors vegetative …

On the role of intracellular potassium in protein synthesis.

The stimulatory effect of signaling on metabolic activity and the metabolic rate studies of ; ; ; ) also argue against a hypometabolic effect induced by food restriction. They studied the oxygen consumption and heat production rates of normally fed controls and worms that were restricted by three dietary restriction (DR) protocols: bacterial dilution in liquid culture, axenic liquid culture and the use of Eat mutants. mutations produce defects in pharyngeal pumping that lead to a reduction in food uptake and concomitant DR phenotypes, including a starved appearance, reduced brood size and extended lifespan. Both proxies of metabolic rate remained unchanged or were elevated in restricted worms. Thus food restriction does not act by lowering the rate of metabolism. At first glance the failure to reduce energy expenditure when food is scarce may seem wasteful. One possible explanation is that there is an increased requirement for synthesis of compounds that are otherwise adequately supplied by food. This is consistent with the lower standing levels of ATP measured in young adult (for about the first 5 days of adulthood) worms grown in axenic culture, which induced the strongest DR phenotype. It is not known if DR animals produce more ROS. DR by all three methods increased SOD and catalase activities, and axenic culture effectively enhanced resistance to thermal and oxidative stress. However, these effects may be part of a complex longevity assurance program that can be induced by a number of unfavorable conditions, including DR, rather than a specific response to increased ROS.

Protein synthesis in halophytes: The influence of potassium, ..

Mutations that compromise the function of the mitochondrial electron transport chain might be predicted to shorten the lifespan but, remarkably, such mutations frequently confer lifespan extension (). In a systematic RNAi screen for genes conferring longevity, genes related to mitochondrial function were over-represented tenfold (). Long-lived worms, in which mitochondrial function was disturbed by RNAi, displayed low ATP levels and oxygen consumption rates compared to appropriate controls. These metabolic phenotypes confirmed an earlier study in which the function of several subunits of the electron transport chain complexes I, III, IV and V were compromised by RNAi knockdown (). These animals were small and showed slow development and behavior (pharyngeal pumping and defecation). Small size, however, is not a universal hallmark of mitochondrial mutants. Hypometabolic mutants, which contain a defect in an iron-sulphur protein subunit of complex III, were reported to have a normal body size (). Some mitochondrial mutants of the Clock family, such as (a gene involved in ubiquinone synthesis) (; review by ) and (involved in the efficiency and fidelity of mitochondrial protein synthesis), are not hypometabolic (; ). Indeed, in mutants complex I activity remains unaltered (; ; ), although this was challenged by ) who found that complex I activity was decreased by approximately 70% while complex II activity was left intact when compared to wild type.

Source of branched chain amino acids (BCAAs) and essential amino acids involved in protein synthesis.
04/11/2017 · On the role of intracellular potassium in protein synthesis Biochim

Plants use potassium in photosynthesis and protein synthesis

The mechanisms by which the animals sense osmotic stress and launch the osmoregulatory response are quite complex. Both disruption of the cuticle and osmotically induced protein damage are believed to induce osmoprotective gene induction. The genes , and several genes are believed to monitor cuticle integrity and to increase glycerol synthesis in response to osmotic stress (). Genome-wide RNAi screening identified 122 genes that suppress the osmotic stress response under normal conditions. When inactivated by RNAi, they cause expression of and glycerol accumulation, attenuating further hypertonic protein damage (). Defective insulin/IGF signaling also contributes to hypertonic stress resistance by increasing the intracellular level of trehalose and activating genes that protect against, or repair, osmotic stress-induced protein damage ().

06/06/2014 · How does potassium help with protein synthesis ..

of insulin and protein synthesis.

Anoxic incubation induces significant increases in the activities of the NADP-dependent isocitrate dehydrogenase, 3-hydroxyacyl-CoA dehydrogenase (HCDH) and, at lower temperatures (10°C), lactate dehydrogenase (). HCDH normally operates in the -oxidation of fatty acids in the mitochondria. ) proposed that a reversed -oxidation pathway results in the synthesis of excretory fatty acids and provides a sink for electrons to maintain the redox balance under anoxia. The glyceraldehyde-3-phosphate dehydrogenase isoenzymes and are also involved in the oxygen-deprivation response, although it is unlikely that they merely enhance the flux through glycolysis (). L-lactate, acetate, succinate and propionate are the main waste products of anaerobic metabolism, and they are predominantly excreted. Malate excretion is substantially reduced under anoxic conditions. Branched fatty acids like 2-methylbutyrate or 2-methylvalyrate, which are typically excreted by parasitic nematodes, are not produced in measurable amounts by anoxic (). reported that ethanol is an important end product of anaerobic fermentation, but ) found ethanol levels to be below the limits of detection. The reason for this discrepancy is not known, but may be related to differences in culture conditions, analytical methods, or possibly to bacterial contamination. Interestingly, anoxic worms cultured axenically excrete more succinate but almost no propionate, suggesting that the enzymes for the conversion of succinate to propionate are not active or are lacking under these conditions. Axenic culture conditions may also affect the lactate carrier, since axenic animals retain most of the lactate produced under anoxia in their tissues (). These metabolic adaptations to oxygen deprivation are consistent with an induction of the pyruvate fermentation and malate dismutation pathways (). Enhanced malate dismutation is also observed during dauer diapause. Dauers are resistant to several environmental stresses, including hypoxia (; ).

Extracellular potassium influences DNA and protein syntheses and glial fibrillary acidic ..

Whey protein can increase GSH synthesis and …

Under aerobic conditions (), will metabolize energy through the standard metabolic pathways. In glycolysis, a series of enzymatic reactions will convert sugars (typically glucose) to pyruvate. During this process, small amounts of ATP are generated and electron carriers are loaded with electrons (NAD+ is reduced to NADH + H+). Consequently, pyruvate is translocated to the mitochondria, decarboxylated and converted into acetyl-CoA. In this process the first completely oxidized carbon is released as CO2. Acetyl-CoA then enters the tricarboxylic acid (TCA) cycle by condensing with oxaloacetate to form citrate. A series of oxidation reactions then ensue with the result that two carbons are expelled as CO2, (G/A)TP is produced and the electron carriers (NAD+ and FAD+) are reduced. Finally, the cycle is completed when oxaloacetate is formed. The electron carriers that were reduced during glycolysis and the TCA cycle deliver their electrons to O2 (with the formation of water) through a series of electron transport chain redox proteins located in the inner mitochondrial membrane. During electron transfer, some of these redox proteins shuttle protons from the mitochondrial matrix to the intramembrane space of the mitochondria, thereby creating an electrochemical gradient. The potential energy in this gradient is finally used by ATP-synthase (another protein complex in the inner mitochondrial membrane) to drive ATP synthesis.