Heat shock proteins do not provide thermoprotection to normal cellular protein synthesis, alpha-amylase mRNA and endoplasmic reticulum lamellae in barley aleurone layers

1996 ◽  
Vol 97 (3) ◽  
pp. 513-523 ◽  
Author(s):  
Daniel F. Lanciloti ◽  
Christopher Cwik ◽  
Mark R. Brodl
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Synthesis ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cellular Protein ◽  
Alpha Amylase ◽  
Barley Aleurone ◽  
Shock Proteins ◽  
Cellular Protein Synthesis

Principles of chaperone-mediated protein folding

1995 ◽  
Vol 348 (1323) ◽  
pp. 107-112 ◽  
Keyword(s):  
Protein Folding ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Chaperones ◽  
Cellular Protein ◽  
Chaperone Proteins ◽  
Shock Proteins ◽  
Polypeptide Chains

The recent discovery of molecular chaperones and their functions has changed dramatically our view of the processes underlying the folding of proteins in vivo . Rather than folding spontaneously, most newly synthesized polypeptide chains seem to acquire their native conformations in a reaction mediated by chaperone proteins. Different classes of molecular chaperones, such as the members of the Hsp70 and Hsp60 families of heat-shock proteins, cooperate in a coordinated pathway of cellular protein folding.

Normal Cellular Protein Synthesis and Heat Shock

1994 ◽  
pp. 61-76 ◽  
Author(s):  
Mark R. Brodl ◽  
Jacqueline D. Campbell ◽  
Kent K. Grindstaff ◽  
Lora Fielding
Keyword(s):  
Protein Synthesis ◽  
Heat Shock ◽  
Cellular Protein ◽  
Cellular Protein Synthesis

scholarly journals Profiling the Expression of Endoplasmic Reticulum Stress Associated Heat Shock Proteins in Animal Epilepsy Models

Neuroscience ◽  
2020 ◽  
Vol 429 ◽  
pp. 156-172 ◽  
Author(s):  
Marta Nowakowska ◽  
Fabio Gualtieri ◽  
Eva-Lotta von Rüden ◽  
Florian Hansmann ◽  
Wolfgang Baumgärtner ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Endoplasmic Reticulum Stress ◽  
Epilepsy Models ◽  
Shock Proteins

Heat shock protein synthesis over time in infective Trichinella spiralis larvae raised in suboptimal culture conditions

2004 ◽  
Vol 78 (3) ◽  
pp. 243-247 ◽  
Author(s):  
J. Martinez ◽  
J. Perez-Serrano ◽  
W.E. Bernadina ◽  
I. Rincon ◽  
F. Rodriguez-Caabeiro
Keyword(s):  
Cell Death ◽  
Protein Synthesis ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Trichinella Spiralis ◽  
Culture Conditions ◽  
Induce Stress ◽  
Shock Proteins ◽  
Over Time

AbstractChanges in the viability, infectivity and heat shock protein (Hsp) levels are reported in Trichinella spiralis first stage larvae (L1) stored in 199 medium for up to seven days at 37°C. These conditions induce stress that the larvae, eventually, cannot overcome. After three days of storage, the infectivity and viability were unchanged, although higher Hsp70 levels were observed. After this time, larvae gradually lost viability and infectivity, coinciding with a decrease in Hsp70 and Hsp90 and an increase in actin (a housekeeping protein). In addition, a possibly inducible heat shock protein, Hsp90i, appeared as constitutive Hsp90 disappeared. No significant changes in Hsp60 levels were detected at any time. These results suggest that heat shock proteins initially try to maintain homeostasis, but on failing, may be involved in cell death.

Heat shock proteins affect RNA processing during the heat shock response of Saccharomyces cerevisiae

1991 ◽  
Vol 11 (2) ◽  
pp. 1062-1068
Author(s):  
H J Yost ◽  
S Lindquist
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Synthesis ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Response ◽  
Rna Splicing ◽  
Yeast Cells ◽  
Yeast Saccharomyces Cerevisiae ◽  
Shock Response ◽  
Shock Proteins

In the yeast Saccharomyces cerevisiae, the splicing of mRNA precursors is disrupted by a severe heat shock. Mild heat treatments prior to severe heat shock protect splicing from disruption, as was previously reported for Drosophila melanogaster. In contrast to D. melanogaster, protein synthesis during the pretreatment is not required to protect splicing in yeast cells. However, protein synthesis is required for the rapid recovery of splicing once it has been disrupted by a sudden severe heat shock. Mutations in two classes of yeast hsp genes affect the pattern of RNA splicing during the heat shock response. First, certain hsp70 mutants, which overproduce other heat shock proteins at normal temperatures, show constitutive protection of splicing at high temperatures and do not require pretreatment. Second, in hsp104 mutants, the recovery of RNA splicing after a severe heat shock is delayed compared with wild-type cells. These results indicate a greater degree of specialization in the protective functions of hsps than has previously been suspected. Some of the proteins (e.g., members of the hsp70 and hsp82 gene families) help to maintain normal cellular processes at higher temperatures. The particular function of hsp104, at least in splicing, is to facilitate recovery of the process once it has been disrupted.

No heat shock protein synthesis is required for induced thermostabilization of translational machinery

1986 ◽  
Vol 6 (6) ◽  
pp. 2267-2270
Author(s):  
R L Hallberg
Keyword(s):  
Protein Synthesis ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Protein Production ◽  
Tetrahymena Thermophila ◽  
Lethal Temperature ◽  
Present Evidence ◽  
Translational Machinery ◽  
Shock Proteins

For Tetrahymena thermophila cells to survive at 43 degrees C, a normally lethal temperature, they require a pretreatment which either elicits the synthesis of heat shock proteins or one which brings about a change in the translational machinery of the cell such that is is not inactivated when transferred to 43 degrees C. In this report I present evidence showing that the latter modification can occur in the complete absence of protein synthesis, indicating that heat shock protein production is not required for the induced thermostabilization of the translational machinery.

scholarly journals Genes for Drosophila small heat shock proteins are regulated differently by ecdysterone.

1991 ◽  
Vol 11 (12) ◽  
pp. 5937-5944 ◽  
Author(s):  
J Amin ◽  
R Mestril ◽  
R Voellmy
Keyword(s):  
Protein Synthesis ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
Transcriptional Level ◽  
Protein Synthesis Inhibitors ◽  
Sequence Elements ◽  
Continuous Presence ◽  
High Level ◽  
Shock Proteins

Genes for small heat shock proteins (hsp27 to hsp22) are activated in late third-instar larvae of Drosophila melanogaster in the absence of heat stress. This regulation has been simulated in cultured Drosophila cells in which the genes are activated by the addition of ecdysterone. Sequence elements (HERE) involved in ecdysterone regulation of the hsp27 and hsp23 genes have been defined by transfection studies and have recently been identified as binding sites for ecdysterone receptor. We report here that the hsp27 and hsp23 genes are regulated differently by ecdysterone. The hsp27 gene is activated rapidly by ecdysterone, even in the absence of protein synthesis. In contrast, high-level expression of the hsp23 gene begins only after a lag of about 6 h, is dependent on the continuous presence of ecdysterone, and is sensitive to low concentrations of protein synthesis inhibitors. Transfection experiments with reporter constructs show that this difference in regulation is at the transcriptional level. Synthetic hsp27 or hsp23 HERE sequences confer hsp27- or hsp23-type ecdysterone regulation on a basal promoter. These findings indicate that the hsp27 gene is a primary, and the hsp23 gene is mainly a secondary, hormone-responsive gene. Ecdysterone receptor is implied to play a role in the regulation of both genes.

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