Transient increase of de novo amino acid synthesis and its physiological significance in water-stressed white clover

2005 ◽  
Vol 32 (9) ◽  
pp. 831 ◽  
Author(s):  
Bok-Rye Lee ◽  
Woo-Jin Jung ◽  
Kil-Yong Kim ◽  
Jean-Christophe Avice ◽  
Alain Ourry ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Water Deficit ◽  
White Clover ◽  
De Novo ◽  
Acid Synthesis ◽  
Ammonia Concentration ◽  
De Novo Synthesis ◽  
Amino Acid Synthesis ◽  
De Novo Protein Synthesis

In white clover (Trifolium repens L. cv. Regal) the kinetics of de novo synthesis of amino acid and protein were compared by tracing 15N under well-watered (control) or water-deficit conditions. The physiological relationship between ammonia concentration, in response to the change in leaf water parameters, and de novo synthesis of amino acid and protein was also assessed. Leaf and root dry mass were not significantly affected for the first 3 d, whereas metabolic parameters such as total N and ammonia were significantly affected within the first day of water-deficit treatment. Inhibitory effect of water deficit on N acquisition from the soil was significant throughout the experimental period. Water deficit induced a significant increase in ammonia concentration in leaves during the first 3 d, and in roots for only the first day. In both leaves and roots, an increase in de novo amino acid synthesis, which peaked in leaves within the first 3 d of water-deficit treatment (Ψw ≥ –1.18 MPa), was observed. The rate of decrease in de novo protein synthesis gradually accelerated as the duration of the water-deficit treatment increased. There was a significant positive relationship between ammonia production and the increase in de novo amino acid synthesis during the first 3-d period, but not during the later period (day 3–day 7). This experiment clearly indicates that the increase in de novo amino acid synthesis caused by water deficit is a transient adaptive response occurring during the first few days and that it is associated with the increased ammonia concentrations, which in turn arise in response to a decrease in de novo protein synthesis.

De novo protein synthesis in relation to ammonia and proline accumulation in water stressed white clover

2004 ◽  
Vol 31 (8) ◽  
pp. 847 ◽  
Author(s):  
Tae-Hwan Kim ◽  
Bok-Rye Lee ◽  
Woo-Jin Jung ◽  
Kil-Yong Kim ◽  
Jean-Christophe Avice ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Water Deficit ◽  
White Clover ◽  
De Novo ◽  
Proline Accumulation ◽  
Leaf Water ◽  
Total N ◽  
Water Parameters ◽  
Leaves And Roots ◽  
De Novo Protein Synthesis

The kinetics of protein incorporation from newly-absorbed nitrogen (N, de novo protein synthesis) was estimated by 15N tracing in 18-week-old white clover plants (Trifolium repens L. cv. Regal) during 7 d of water-deficit treatment. The physiological relationship between kinetics and accumulation of proline and ammonia in response to the change in leaf-water parameters was also assessed. All leaf-water parameters measured decreased gradually under water deficit. Leaf and root dry mass was not significantly affected during the first 3 d when decreases in leaf-water parameters were substantial. However, metabolic parameters such as total N, proline and ammonia were significantly affected within 1 d of commencement of water-deficit treatment. Water-deficit treatment significantly increased the proline and NH3–NH4+ concentrations in both leaves and roots. There was a marked reduction in the amount of N incorporated into the protein fraction from the newly absorbed N (NANP) in water-deficit stressed plants, particularly in leaf tissue. This reduction in NANP was strongly associated with an increased concentration of NH3–NH4+ in roots (P≤0.05) and proline (P≤0.01) in leaves and roots. These results suggest that proline accumulation may be a sensitive biochemical indicator of plant water status and of the dynamics of de novo protein synthesis in response to stress severity.

scholarly journals Proteasome Inhibition in Brassica napus Roots Increases Amino Acid Synthesis to Offset Reduced Proteolysis

2020 ◽  
Vol 61 (6) ◽  
pp. 1028-1040
Author(s):  
Dan Pereksta ◽  
Dillon King ◽  
Fahmida Saki ◽  
Amith Maroli ◽  
Elizabeth Leonard ◽  
...  
Keyword(s):  
Amino Acid ◽  
Brassica Napus ◽  
De Novo ◽  
Metabolic Response ◽  
Sugar Metabolism ◽  
Proteasome Inhibition ◽  
Acid Synthesis ◽  
Amino Acid Synthesis ◽  
Amino Acid Depletion ◽  
Metabolic Activities

Abstract Cellular homeostasis is maintained by the proteasomal degradation of regulatory and misfolded proteins, which sustains the amino acid pool. Although proteasomes alleviate stress by removing damaged proteins, mounting evidence indicates that severe stress caused by salt, metal(oids), and some pathogens can impair the proteasome. However, the consequences of proteasome inhibition in plants are not well understood and even less is known about how its malfunctioning alters metabolic activities. Lethality causes by proteasome inhibition in non-photosynthetic organisms stem from amino acid depletion, and we hypothesized that plants respond to proteasome inhibition by increasing amino acid biosynthesis. To address these questions, the short-term effects of proteasome inhibition were monitored for 3, 8 and 48 h in the roots of Brassica napus treated with the proteasome inhibitor MG132. Proteasome inhibition did not affect the pool of free amino acids after 48 h, which was attributed to elevated de novo amino acid synthesis; these observations coincided with increased levels of sulfite reductase and nitrate reductase activities at earlier time points. However, elevated amino acid synthesis failed to fully restore protein synthesis. In addition, transcriptome analysis points to perturbed abscisic acid signaling and decreased sugar metabolism after 8 h of proteasome inhibition. Proteasome inhibition increased the levels of alternative oxidase but decreased aconitase activity, most sugars and tricarboxylic acid metabolites in root tissue after 48 h. These metabolic responses occurred before we observed an accumulation of reactive oxygen species. We discuss how the metabolic response to proteasome inhibition and abiotic stress partially overlap in plants.

scholarly journals Target of Rapamycin Inhibition in Chlamydomonas reinhardtii Triggers de Novo Amino Acid Synthesis by Enhancing Nitrogen Assimilation

2018 ◽  
Vol 30 (10) ◽  
pp. 2240.1-2254 ◽  
Author(s):  
Umarah Mubeen ◽  
Jessica Jüppner ◽  
Jessica Alpers ◽  
Dirk K. Hincha ◽  
Patrick Giavalisco
Keyword(s):  
Amino Acid ◽  
Chlamydomonas Reinhardtii ◽  
Nitrogen Assimilation ◽  
De Novo ◽  
Acid Synthesis ◽  
Target Of Rapamycin ◽  
Amino Acid Synthesis

scholarly journals Mechanism of De Novo Branched-Chain Amino Acid Synthesis as an Alternative Electron Sink in Hypoxic Aspergillus nidulans Cells

2010 ◽  
Vol 76 (5) ◽  
pp. 1507-1515 ◽  
Author(s):  
Motoyuki Shimizu ◽  
Tatsuya Fujii ◽  
Shunsuke Masuo ◽  
Naoki Takaya
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Aspergillus Nidulans ◽  
De Novo ◽  
Acid Synthesis ◽  
Branched Chain Amino Acids ◽  
Amino Acid Synthesis ◽  
Lactate Dehydrogenase Activity ◽  
Branched Chain Amino Acid ◽  
Branched Chain

ABSTRACT Although branched-chain amino acids are synthesized as building blocks of proteins, we found that the fungus Aspergillus nidulans excretes them into the culture medium under hypoxia. The transcription of predicted genes for synthesizing branched-chain amino acids was upregulated by hypoxia. A knockout strain of the gene encoding the large subunit of acetohydroxy acid synthase (AHAS), which catalyzes the initial reaction of the synthesis, required branched-chain amino acids for growth and excreted very little of them. Pyruvate, a substrate for AHAS, increased the amount of hypoxic excretion in the wild-type strain. These results indicated that the fungus responds to hypoxia by synthesizing branched-chain amino acids via a de novo mechanism. We also found that the small subunit of AHAS regulated hypoxic branched-chain amino acid production as well as cellular AHAS activity. The AHAS knockout resulted in higher ratios of NADH/NAD+ and NADPH/NADP+ under hypoxia, indicating that the branched-chain amino acid synthesis contributed to NAD+ and NADP+ regeneration. The production of branched-chain amino acids and the hypoxic induction of involved genes were partly repressed in the presence of glucose, where cells produced ethanol and lactate and increased levels of lactate dehydrogenase activity. These indicated that hypoxic branched-chain amino acid synthesis is a unique alternative mechanism that functions in the absence of glucose-to-ethanol/lactate fermentation and oxygen respiration.

Transmembrane transport and intracellular kinetics of amino acids in human skeletal muscle

1995 ◽  
Vol 268 (1) ◽  
pp. E75-E84 ◽  
Author(s):  
G. Biolo ◽  
R. Y. Fleming ◽  
S. P. Maggi ◽  
R. R. Wolfe
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Human Skeletal Muscle ◽  
De Novo ◽  
Transmembrane Transport ◽  
Acid Transport ◽  
De Novo Synthesis ◽  
Intracellular Amino Acid

We have used stable isotopic tracers of amino acids to measure in vivo transmembrane transport of phenylalanine, leucine, lysine, alanine, and glutamine as well as the rates of intracellular amino acid appearance from proteolysis, de novo synthesis, and disappearance to protein synthesis in human skeletal muscle. Calculations were based on data obtained by the arteriovenous catheterization of the femoral vessels and muscle biopsy. We found that the fractional contribution of transport from the bloodstream to the total intracellular amino acid appearance depends on the individual amino acid, varying between 0.63 +/- 0.02 for phenylalanine and 0.22 +/- 0.02 for alanine. Rates of alanine and glutamine de novo synthesis were approximately eight and five times their rate of appearance from protein breakdown, respectively. The model-derived rate of protein synthesis was highly correlated with the same value calculated by means of the tracer incorporation technique. Furthermore, amino acid transport rates were in the range expected from literature values. Consequently, we conclude that our new model provides a valid means of quantifying the important aspects of protein synthesis, breakdown, and amino acid transport in human subjects.

Glucose and insulin effects on de novo amino acid synthesis in young men: Studies with stable isotope labeled alanine, glycine, leucine, and lysine

Metabolism ◽  
1982 ◽  
Vol 31 (12) ◽  
pp. 1210-1218 ◽  
Author(s):  
Jean-Jacques Robert ◽  
Dennis M. Bier ◽  
X.H. Zhao ◽  
Dwight E. Matthews ◽  
Vernon R. Young
Keyword(s):  
Amino Acid ◽  
Stable Isotope ◽  
De Novo ◽  
Young Men ◽  
Acid Synthesis ◽  
Amino Acid Synthesis

scholarly journals De novo amino acid synthesis and turnover during N2 fixation

2017 ◽  
Vol 63 (3) ◽  
pp. 1076-1092 ◽  
Author(s):  
Natalie Loick-Wilde ◽  
Sarah C. Weber ◽  
Elvita Eglite ◽  
Iris Liskow ◽  
Detlef Schulz-Bull ◽  
...  
Keyword(s):  
Amino Acid ◽  
N2 Fixation ◽  
De Novo ◽  
Acid Synthesis ◽  
Amino Acid Synthesis

Whole Body De Novo Amino Acid Synthesis in Type I (Insulin-dependent) Diabetes Studied With Stable Isotope-labeled Leucine, Alanine, and Glycine

Diabetes ◽  
1985 ◽  
Vol 34 (1) ◽  
pp. 67-73 ◽  
Author(s):  
J. J. Robert ◽  
B. Beaufrere ◽  
J. Koziet ◽  
J. F. Desjeux ◽  
D. M. Bier ◽  
...  
Keyword(s):  
Amino Acid ◽  
Stable Isotope ◽  
De Novo ◽  
Acid Synthesis ◽  
Insulin Dependent Diabetes ◽  
Whole Body ◽  
Type I ◽  
Amino Acid Synthesis ◽  
Insulin Dependent

Pyruvate metabolism by Anaplasma marginale in cell-free culture

1999 ◽  
Vol 45 (2) ◽  
pp. 185-189 ◽  
Author(s):  
Linda E McHolland ◽  
Daniel R Caldwell
Keyword(s):  
Amino Acid ◽  
De Novo ◽  
Anaplasma Marginale ◽  
Acid Synthesis ◽  
Pyruvate Metabolism ◽  
Amino Acid Synthesis ◽  
Free System ◽  
Label Incorporation ◽  
A Cell ◽  
Body Components

Partially purified Anaplasma marginale initial bodies were cultivated in a cell-free system in the presence of [3-14C]pyruvate for 24 or 48 h. Experiments showed that a significant portion of the pyruvate supplied to the cultures was incorporated into initial body components. Label incorporation was reduced by 72% in the presence of oxytetracycline. Fractionation and chromatography of the organisms revealed radioactive incorporation as alanine. This is the first report of de novo amino acid synthesis by A. marginale demonstrating that the rickettsia is capable of using pyruvate, an erythrocyte glycolytic product, in its metabolism.Key words: Anaplasma marginale, pyruvate metabolism, amino acid synthesis.

scholarly journals Development, amino acid utilization and cell allocation in bovine embryos after in vitro production in contrasting culture systems

Reproduction ◽  
2002 ◽  
pp. 155-165 ◽  
Author(s):  
M Kuran ◽  
JJ Robinson ◽  
DS Brown ◽  
TG McEvoy
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
De Novo ◽  
Acid Uptake ◽  
Free Medium ◽  
Cell Counts ◽  
De Novo Protein Synthesis ◽  
Amino Acid Flux ◽  
Protein Free Medium

The effects of protein-supplemented and protein-free media on amino acid uptake, protein synthesis and cell differentiation in bovine blastocysts were investigated. Four formulations of synthetic oviduct fluid were used. Each formulation was identified by the principal supplement: bovine serum albumin (0.4%, w/v); polyvinyl alcohol (0.3%, w/v); or either of two steer sera (10%, v/v). After zygote culture, blastocyst yields (day 7.5) were lowest in protein-free medium and highest in albumin-supplemented medium. Subsequent 12 h incubation in the presence of both essential and non-essential amino acids was used for the measurement of amino acid flux. All blastocysts released alanine but consumed aspartate (P < 0.001) and the extent was influenced by prior culture conditions. Aspartate uptake was lower in blastocysts produced in protein-free conditions (P < 0.05) than in blastocysts produced in albumin-supplemented conditions. Consumption indices for 16 other amino acids were not influenced by blastocyst source. Cell counts and hatching incidences were highest for albumin-supplemented blastocysts, but were similar among blastocysts from the protein-free and serum-dependent treatments. Crucially, the use of protein-free medium for zygote culture did not compromise resultant blastocysts in terms of either de novo protein synthesis ([3H]phenylalanine incorporation) or trophectoderm function (phenotype based on interferon-tau detection). Thus, although blastocyst yields were compromised after zygote culture in a protein-free (vis-a-vis albumin-supplemented) medium, amino acid flux was qualitatively conserved, and only quantitatively modified in the case of alanine and aspartate. Moreover, vital properties of blastocysts that were produced, including de novo protein synthesis and trophectodermal cell function, apparently were not adversely affected by protein deprivation.

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