Changes in Free Amino Acids and Stress Protein Synthesis in Two Genotypes of Green Gram under Salt Stress

2005 ◽  
Vol 1 (1) ◽  
pp. 56-66 ◽  
Author(s):  
Neelam Misra . ◽  
Ajay Kumar Gupta . ◽  
U.N. Dwivedi .
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Salt Stress ◽  
Free Amino Acids ◽  
Free Amino ◽  
Stress Protein ◽  
Green Gram

scholarly journals Amino acid regulation of synthesis of ribonucleic acid and protein in the liver of rats

1971 ◽  
Vol 124 (2) ◽  
pp. 385-392 ◽  
Author(s):  
R. W. Wannemacher ◽  
C. F. Wannemacher ◽  
M. B. Yatvin
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Free Amino Acids ◽  
Free Amino ◽  
Cellular Protein ◽  
Deficient Diet ◽  
Cellular Protein Content ◽  
Regulate Protein

Weanling (23-day-old) rats were fed on either a low-protein diet (6% casein) or a diet containing an adequate amount of protein (18% casein) for 28 days. Hepatic cells from animals fed on the deficient diet were characterized by markedly lower concentrations of protein and RNA in all cellular fractions as compared with cells from control rats. The bound rRNA fraction was decreased to the greatest degree, whereas the free ribosomal concentrations were only slightly less than in control animals. A good correlation was observed between the rate of hepatic protein synthesis in vivo and the cellular protein content of the liver. Rates of protein synthesis both in vivo and in vitro were directly correlated with the hepatic concentration of individual free amino acids that are essential for protein synthesis. The decreased protein-synthetic ability of the ribosomes from the liver of protein-deprived rats was related to a decrease in the number of active ribosomes and heavy polyribosomes. The lower ribosomal content of the hepatocytes was correlated with the decreased concentration of essential free amino acids. In the protein-deprived rats, the rate of accumulation of newly synthesized cytoplasmic rRNA was markedly decreased compared with control animals. From these results it was concluded that amino acids regulate protein synthesis (1) by affecting the number of ribosomes that actively synthesize protein and (2) by inhibiting the rate of synthesis of new ribosomes. Both of these processes may involve the synthesis of proteins with a rapid rate of turnover.

scholarly journals Transcriptomic Analysis of Short-Term Salt Stress Response in Watermelon Seedlings

2020 ◽  
Vol 21 (17) ◽  
pp. 6036
Author(s):  
Qiushuo Song ◽  
Madhumita Joshi ◽  
Vijay Joshi
Keyword(s):  
Amino Acids ◽  
Salt Stress ◽  
Amino Acid ◽  
Photosystem Ii ◽  
Free Amino Acids ◽  
Free Amino ◽  
Molecular Mechanisms ◽  
Differentially Expressed ◽  
Short Term ◽  
Salt Stress Response

Watermelon (Citrullus lanatus L.) is a widely popular vegetable fruit crop for human consumption. Soil salinity is among the most critical problems for agricultural production, food security, and sustainability. The transcriptomic and the primary molecular mechanisms that underlie the salt-induced responses in watermelon plants remain uncertain. In this study, the photosynthetic efficiency of photosystem II, free amino acids, and transcriptome profiles of watermelon seedlings exposed to short-term salt stress (300 mM NaCl) were analyzed to identify the genes and pathways associated with response to salt stress. We observed that the maximal photochemical efficiency of photosystem II decreased in salt-stressed plants. Most free amino acids in the leaves of salt-stressed plants increased many folds, while the percent distribution of glutamate and glutamine relative to the amino acid pool decreased. Transcriptome analysis revealed 7622 differentially expressed genes (DEGs) under salt stress, of which 4055 were up-regulated. The GO analysis showed that the molecular function term “transcription factor (TF) activity” was enriched. The assembled transcriptome demonstrated up-regulation of 240 and down-regulation of 194 differentially expressed TFs, of which the members of ERF, WRKY, NAC bHLH, and MYB-related families were over-represented. The functional significance of DEGs associated with endocytosis, amino acid metabolism, nitrogen metabolism, photosynthesis, and hormonal pathways in response to salt stress are discussed. The findings from this study provide novel insights into the salt tolerance mechanism in watermelon.

scholarly journals Pinocytosis and intracellular degradation of exogenous protein: modulation by amino acids.

1983 ◽  
Vol 96 (6) ◽  
pp. 1586-1591 ◽  
Author(s):  
J M Besterman ◽  
J A Airhart ◽  
R B Low ◽  
D E Rannels
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Free Amino Acids ◽  
Free Amino ◽  
De Novo ◽  
Serum Proteins ◽  
Fluid Phase ◽  
Cellular Protein ◽  
Intracellular Degradation ◽  
Exogenous Protein

Intracellular degradation of exogenous (serum) proteins provides a source of amino acids for cellular protein synthesis. Pinocytosis serves as the mechanism for delivering exogenous protein to the lysosomes, the major site of intracellular degradation of exogenous protein. To determine whether the availability of extracellular free amino acids altered pinocytic function, we incubated monolayers of pulmonary alveolar macrophages with the fluid-phase marker, [14C]sucrose, and we dissected the pinocytic process by kinetic analysis. Additionally, intracellular degradation of endogenous and exogenous protein was monitored by measuring phenylalanine released from the cell monolayers in the presence of cycloheximide. Results revealed that in response to a subphysiological level of essential amino acids or to amino acid deprivation, (a) the rate of fluid-phase pinocytosis increased in such a manner as to preferentially increase both delivery to and size of an intracellular compartment believed to be the lysosomes, (b) the degradation of exogenously supplied albumin increased, and (c) the fraction of phenylalanine derived from degradation of exogenous albumin and reutilized for de novo protein synthesis increased. Thus, modulation of the pinosome-lysosome pathway may represent a homeostatic mechanism sensitive to the availability of extracellular free amino acids.

scholarly journals Free amino acids and glycine betaine in leaf osmoregulation of spinach responding to increasing salt stress

2003 ◽  
Vol 158 (3) ◽  
pp. 455-463 ◽  
Author(s):  
Catello Di Martino ◽  
Sebastiano Delfine ◽  
Roberto Pizzuto ◽  
Francesco Loreto ◽  
Amodio Fuggi
Keyword(s):  
Amino Acids ◽  
Salt Stress ◽  
Glycine Betaine ◽  
Free Amino Acids ◽  
Free Amino

scholarly journals The specific radioactivity of the precursor pool for estimates of the rate of protein synthesis (Short Communication)

1973 ◽  
Vol 134 (4) ◽  
pp. 1127-1130 ◽  
Author(s):  
Edward B. Fern ◽  
Peter J. Garlick
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Free Amino Acids ◽  
Free Amino ◽  
Short Communication ◽  
Specific Radioactivity ◽  
Precursor Pool

Infusion of rats with [U-14C]glycine resulted in labelling of glycine and serine in tissue proteins. The pattern of labelling in protein more nearly resembled that of the free amino acids in the tissue than in the plasma.

Autoradiographische Untersuchungen zur Proteinsynthese während der Frühentwicklung von Dermestes frischi (Coleoptera) / Autoradiographic Investigations on Protein Synthesis During Early Development of Dermestes frischi (Coleoptera)

1972 ◽  
Vol 27 (2) ◽  
pp. 193-195 ◽  
Author(s):  
H. W. Küthe
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Early Development ◽  
Free Amino Acids ◽  
Free Amino ◽  
Protein Fractions ◽  
Cleavage Stages ◽  
Cortical Regions

Injection of tritiated phenylalanine or leucine in eggs shortly after deposition shows the importance and use of free amino acids during cleavage stages. First the activity is found homogeneously distributed in the yolk system and ooplasm. In late cleavage stages the amino acids are incorporated into the periplasm of the egg. These results lead to the conclusions, that there is a continuous transfer of material out of the yolk system into cortical regions during cleavage. Secondly the first new synthetized protein fractions are located in the cortical ooplasm.

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