Heat shock and recovery in aged wheat aleurone layers

1993 ◽  
Vol 3 (3) ◽  
pp. 179-186 ◽  
Author(s):  
M.A. Livesley ◽  
C. M. Bray
Keyword(s):  
Heat Shock ◽  
Recovery Period ◽  
Pulse Labelling ◽  
Amino Acid Incorporation ◽  
Control Of Gene Expression ◽  
Acid Incorporation ◽  
Seed Ageing ◽  
Aged Seed ◽  
Wheat Seeds ◽  
Germinated Seeds

AbstractAgeing of wheat seeds (Triticum aestivum cv. Galahad, 1986 harvest) during storage is accompanied by an increase in the proportion of abnormal seedlings produced when aged seed lots germinate. The response of aleurone layers from normally and abnormally germinated seeds to heat shock has been investigated. [14C]-amino acid incorporation into aleurone layers from 3-d normally and abnormally germinated seeds diminished after 4 h at 42°C but the aleurone layers were able to recover significantly during a 5-h period at 20°C following heat shock. [35S]-methionine pulse-labelling of aleurone proteins showed that α-amylase isoenzyme synthesis was abolished upon heat shock in aleurone layers for both normally and abnormally germinated seeds and that only aleurone layers from normally germinated seeds were capable of recommencing substantial α-amylase synthesis during the recovery period. Heat shock caused aleurone layers from abnormally germinated seeds to synthesize polypeptides not synthesized by aleurone layers from normally germinated seeds under the same conditions. The synthesis of certain polypeptides by aleurone layers from abnormally germinated seeds was enhanced at 20°C, 42°C and during recovery compared with normally germinated seeds. These results are discussed in terms of the control of gene expression during heat shock and recovery during seed ageing.

Heat shock-induced acquisition of thermotolerance at the levels of cell survival and translation in Xenopus A6 kidney epithelial cells

1999 ◽  
Vol 77 (2) ◽  
pp. 141-151 ◽  
Author(s):  
Donna Phang ◽  
Elizabeth M Joyce ◽  
John J Heikkila
Keyword(s):  
Heat Shock ◽  
Xenopus Laevis ◽  
Cell Survival ◽  
Recovery Period ◽  
Epithelial Cell Line ◽  
Amino Acid Incorporation ◽  
A6 Cells ◽  
Acid Incorporation ◽  
Survival Studies ◽  
Shock Proteins

In this study we have investigated the acquisition of thermotolerance in a Xenopus laevis kidney A6 epithelial cell line at both the level of cell survival and translation. In cell survival studies, A6 cells were incubated at temperatures ranging from 22 to 35°C for 2 h followed by a thermal challenge at 39°C for 2 h and a recovery period at 22°C for 24 h. Optimal acquisition of thermotolerance occurred at 33°C. For example, exposure of A6 cells to 39°C for 2 h resulted in only 3.4% survival of the cells whereas prior exposure to 33°C for 2 h enhanced the survival rate to 69%. This state of thermotolerance in A6 cells was detectable after 1 h at 33°C and was maintained even after 18 h of incubation. Cycloheximide inhibited the acquisition of thermotolerance at 33°C suggesting the requirement for ongoing protein synthesis. The optimal temperature for the acquisition of translational thermotolerance also occurred at 33°C. Treatment of A6 cells at 39°C for 2 h resulted in an inhibition of labeled amino acid incorporation into protein which recovered to approximately 14% of control after 19 h at 22°C whereas cells treated at 33°C for 2 h prior to the thermal challenge recovered to 58% of control levels. These translationally thermotolerant cells displayed relatively high levels of the heat shock proteins hsp30, hsp70, and hsp90 compared to pretreatment at 22, 28, 30, or 35°C. These studies demonstrate that Xenopus A6 cells can acquire a state of thermotolerance and that it is correlated with the synthesis of heat shock proteins.Key words: Xenopus laevis, heat shock protein, hsps, A6 cells, chaperone, thermotolerance.

scholarly journals Cerebral Protein Synthesis during Long-Term Recovery from Severe Hypoglycemia

1986 ◽  
Vol 6 (1) ◽  
pp. 42-51 ◽  
Author(s):  
Marika Kiessling ◽  
Roland N. Auer ◽  
Paul Kleihues ◽  
Bo K. Siesjö
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Dentate Gyrus ◽  
Granule Cells ◽  
Recovery Period ◽  
Severe Hypoglycemia ◽  
Amino Acid Incorporation ◽  
Acid Incorporation ◽  
Increased Risk

Regional protein synthesis was investigated in the rat brain during long-term recovery from insulin-induced hypoglycemia with 30 min of cerebral electrical silence. At various time intervals up to 14 days after glucose replenishment, animals received a single dose of L-[3, 5-3H]tyrosine and were killed 30 min later. Brains were processed for autoradiography using the stripping film technique. Although hypoglycemia sufficiently severe to cause cessation of EEG activity leads to almost complete inhibition of amino acid incorporation in all “vulnerable” forebrain structures (cerebral cortex, hippocampus, caudoputamen), autoradiographs revealed a very specialized sequence with differential posthypoglycemic restoration of biosynthetic activity in certain neuronal cell types. Three major subpopulations could be distinguished: Neurons that fully regained their protein synthetic capacity within 6 h following hypoglycemia (cortical neurons of layer III–VI, large neurons in the caudoputamen, CA3 and CA4 pyramidal neurons, the majority of granule cells of the dentate gyrus) seemed to escape neuronal necrosis. Prolonged impairment of protein synthesis with only partial restoration during the early posthypoglycemic recovery period (CA1 neurons, most small- to medium-sized neurons of the caudoputamen) carried an increased risk of permanent cell damage. The large majority of these neurons, however, showed full recovery of protein synthesis as late as 7 days after hypoglycemia. Neurons with complete lack of amino acid incorporation after 6 h of recovery (granule cells at the crest of the dentate gyrus, small neurons of the dorsolateral caudoputamen) never resumed protein synthesis, regressed, and died. These studies in conjunction with morphological analysis indicate that the sequential recovery of protein synthesis reflects the extent to which neuronal populations are at risk during severe hypoglycemia.

scholarly journals Transferability of N-terminal mutations of pyrrolysyl-tRNA synthetase in one species to that in another species on unnatural amino acid incorporation efficiency

Amino Acids ◽  
2020 ◽  
Author(s):  
Thomas L. Williams ◽  
Debra J. Iskandar ◽  
Alexander R. Nödling ◽  
Yurong Tan ◽  
Louis Y. P. Luk ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Genetic Code ◽  
Unnatural Amino Acids ◽  
Trna Synthetase ◽  
Unnatural Amino Acid ◽  
Amino Acid Incorporation ◽  
Acid Incorporation ◽  
Genetic Code Expansion ◽  
Incorporation Efficiency

AbstractGenetic code expansion is a powerful technique for site-specific incorporation of an unnatural amino acid into a protein of interest. This technique relies on an orthogonal aminoacyl-tRNA synthetase/tRNA pair and has enabled incorporation of over 100 different unnatural amino acids into ribosomally synthesized proteins in cells. Pyrrolysyl-tRNA synthetase (PylRS) and its cognate tRNA from Methanosarcina species are arguably the most widely used orthogonal pair. Here, we investigated whether beneficial effect in unnatural amino acid incorporation caused by N-terminal mutations in PylRS of one species is transferable to PylRS of another species. It was shown that conserved mutations on the N-terminal domain of MmPylRS improved the unnatural amino acid incorporation efficiency up to five folds. As MbPylRS shares high sequence identity to MmPylRS, and the two homologs are often used interchangeably, we examined incorporation of five unnatural amino acids by four MbPylRS variants at two temperatures. Our results indicate that the beneficial N-terminal mutations in MmPylRS did not improve unnatural amino acid incorporation efficiency by MbPylRS. Knowledge from this work contributes to our understanding of PylRS homologs which are needed to improve the technique of genetic code expansion in the future.

scholarly journals FRUCTOSE-AMINO ACIDS IN LIVER: STIMULI OF AMINO ACID INCORPORATION IN VITRO

1955 ◽  
Vol 215 (1) ◽  
pp. 111-124 ◽  
Author(s):  
Henry Borsook ◽  
Adolph Abrams ◽  
Peter H. Lowy
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Incorporation ◽  
Acid Incorporation

scholarly journals INDEPENDENT ANTAGONISM OF AMINO ACID INCORPORATION INTO PROTEIN

1954 ◽  
Vol 210 (2) ◽  
pp. 837-849 ◽  
Author(s):  
M. Rabinovitz ◽  
Margaret E. Olson ◽  
David M. Greenberg
Keyword(s):  
Amino Acid ◽  
Amino Acid Incorporation ◽  
Acid Incorporation
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