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 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.

Characterization of a Tetrahymena thermophila mutant strain unable to develop normal thermotolerance

1986 ◽  
Vol 6 (11) ◽  
pp. 3854-3861
Author(s):  
K W Kraus ◽  
E M Hallberg ◽  
R Hallberg
Keyword(s):  
Protein Synthesis ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Mutant Strain ◽  
Tetrahymena Thermophila ◽  
Translational Machinery ◽  
Associated Functions ◽  
Normal Functional ◽  
Drug Treatments ◽  
Shock Proteins

For Tetrahymena thermophila cells to survive extended periods of time at 43 degrees C, they must continuously synthesize heat shock proteins. For its translational machinery to function at 43 degrees C, T. thermophila requires either prior nonlethal heat shock treatment or brief treatment with partially inhibiting doses of cycloheximide or emetine. We have identified and characterized a mutant strain of T. thermophila (MC-3) in which prior nonlethal heat shock does not prevent protein synthesis inactivation at 43 degrees C. In addition, treatment of MC-3 cells with either of the antibiotics that normally confer 43 degrees C thermoprotection on wild-type cells elicited no similar thermoprotective response in these cells. Despite these phenotypic characteristics, by other criteria MC-3 synthesized a normal, functional array of heat shock proteins at 40 degrees C, a nonlethal heat shock protein-inducing temperature. The mutation in MC-3 which prevents the thermostabilization of protein synthesis by nonlethal heat shock is, by genetic criteria, most likely the same one which prevents the induction of thermotolerance by drug treatments. We present evidence that this mutation may affect some ribosome-associated functions.

scholarly journals Characterization of a Tetrahymena thermophila mutant strain unable to develop normal thermotolerance.

1986 ◽  
Vol 6 (11) ◽  
pp. 3854-3861 ◽  
Author(s):  
K W Kraus ◽  
E M Hallberg ◽  
R Hallberg
Keyword(s):  
Protein Synthesis ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Mutant Strain ◽  
Tetrahymena Thermophila ◽  
Translational Machinery ◽  
Associated Functions ◽  
Normal Functional ◽  
Drug Treatments ◽  
Shock Proteins

For Tetrahymena thermophila cells to survive extended periods of time at 43 degrees C, they must continuously synthesize heat shock proteins. For its translational machinery to function at 43 degrees C, T. thermophila requires either prior nonlethal heat shock treatment or brief treatment with partially inhibiting doses of cycloheximide or emetine. We have identified and characterized a mutant strain of T. thermophila (MC-3) in which prior nonlethal heat shock does not prevent protein synthesis inactivation at 43 degrees C. In addition, treatment of MC-3 cells with either of the antibiotics that normally confer 43 degrees C thermoprotection on wild-type cells elicited no similar thermoprotective response in these cells. Despite these phenotypic characteristics, by other criteria MC-3 synthesized a normal, functional array of heat shock proteins at 40 degrees C, a nonlethal heat shock protein-inducing temperature. The mutation in MC-3 which prevents the thermostabilization of protein synthesis by nonlethal heat shock is, by genetic criteria, most likely the same one which prevents the induction of thermotolerance by drug treatments. We present evidence that this mutation may affect some ribosome-associated functions.

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.

Temperature-dependent pattern of heat shock protein synthesis in psychrophilic and psychrotrophic microorganisms

1986 ◽  
Vol 32 (6) ◽  
pp. 516-521 ◽  
Author(s):  
Kirk L. McCallum ◽  
John J. Heikkila ◽  
William E. Inniss
Keyword(s):  
Protein Synthesis ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Incubation Temperature ◽  
The Arctic ◽  
Transcriptional Level ◽  
Psychrophilic Bacterium ◽  
Temperature Dependent ◽  
Shock Proteins

The patterns of proteins synthesized by the arctic psychrophilic bacterium Res-10 and the psychrotroph Bacillus psychrophilus during various heat shocks up to 32 °C were examined. Both microorganisms were found to display temperature-dependent patterns of heat shock protein synthesis. Elevation of the incubation temperature of the arctic psychrophile from 0 to 15, 20, 25, or 32 °C induced the synthesis of at least 19 heat shock proteins. Imposing similar heat shock upon cells of the psychrotroph resulted in the induction of at least 25 heat shock proteins. Examination of the effect of the transcriptional inhibitor rifampicin on the synthesis of heat shock proteins revealed that the primary control of heat shock protein synthesis lies at the transcriptional level in both microorganisms.

scholarly journals Cross-priming of minor histocompatibility antigen-specific cytotoxic T cells upon immunization with the heat shock protein gp96.

1995 ◽  
Vol 182 (3) ◽  
pp. 885-889 ◽  
Author(s):  
D Arnold ◽  
S Faath ◽  
H Rammensee ◽  
H Schild
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Tumor Cells ◽  
Mhc Class I ◽  
Donor Cell ◽  
Class I ◽  
Heat Shock Protein Gp96 ◽  
Shock Proteins

Vaccination of mice with heat shock proteins isolated from tumor cells induces immunity to subsequent challenge with those tumor cells the heat shock protein was isolated from but not with other tumor cells (Udono, H., and P.K. Srivastava. 1994. J. Immunol. 152:5398-5403). The specificity of this immune response is caused by tumor-derived peptides bound to the heat shock proteins (Udono., H., and P.K. Srivastava. 1993. J. Exp. Med. 178:1391-1396). Our experiments show that a single immunization with the heat shock protein gp96 isolated from beta-galactosidase (beta-gal) expressing P815 cells (of DBA/2 origin) induces cytotoxic T lymphocytes (CTLs) specific for beta-gal, in addition to minor H antigens expressed by these cells. CTLs can be induced in mice that are major histocompatibility complex (MHC) identical to the gp96 donor cells (H-2d) as well as in mice with a different MHC (H-2b). Thus gp96 is able to induce "cross priming" (Matzinger, P., and M.J. Bevan. 1977. Cell. Immunol. 33:92-100), indicating that gp96-associated peptides are not limited to the MHC class I ligands of the gp96 donor cell. Our data confirm the notion that samples of all cellular antigens presentable by MHC class I molecules are represented by peptides associated with gp96 molecules of that cell, even if the fitting MHC molecule is not expressed. In addition, we extend previous reports on the in vivo immunogenicity of peptides associated gp96 molecules to two new groups of antigens, minor H antigens, and proteins expressed in the cytosol.

Progesterone enhances target gene transcription by receptor free of heat shock proteins hsp90, hsp56, and hsp70

1991 ◽  
Vol 11 (10) ◽  
pp. 4998-5004
Author(s):  
M K Bagchi ◽  
S Y Tsai ◽  
M J Tsai ◽  
B W O'Malley
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Transcriptional Activation ◽  
Target Gene ◽  
Steroid Hormone ◽  
Receptor Activation ◽  
Target Cells ◽  
Dependent Manner ◽  
Shock Proteins

Steroid receptors regulate transcription of target genes in vivo and in vitro in a steroid hormone-dependent manner. Unoccupied progesterone receptor exists in the low-salt homogenates of target cells as a functionally inactive 8 to 10S complex with several nonreceptor components such as two molecules of 90-kDa heat shock protein (hsp90), a 70-kDa heat shock protein (hsp70), and a 56-kDa heat shock protein (hsp56). Ligand-induced dissociation of receptor-associated proteins such as hsp90 has been proposed as the mechanism of receptor activation. Nevertheless, it has not been established whether, beyond release of heat shock proteins, the steroidal ligand plays a role in modulating receptor activity. To examine whether the release of these nonreceptor proteins from receptor complex results in a constitutively active receptor, we isolated an unliganded receptor form essentially free of hsp90, hsp70, and hsp56. Using a recently developed steroid hormone-responsive cell-free transcription system, we demonstrate for the first time that the dissociation of heat shock proteins is not sufficient to generate a functionally active receptor. This purified receptor still requires hormone for high-affinity binding to a progesterone response element and for efficient transcriptional activation of a target gene. When an antiprogestin, Ru486, is bound to the receptor, it fails to promote efficient transcription. We propose that in the cell, in addition to the release of receptor-associated inhibitory proteins, a distinct hormone-mediated activation event must precede efficient gene activation.

A family of related proteins is encoded by the major Drosophila heat shock gene family

1982 ◽  
Vol 2 (3) ◽  
pp. 286-292
Author(s):  
S C Wadsworth
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Sodium Dodecyl ◽  
Heat Shock Gene ◽  
Partial Digestion ◽  
Shock Gene ◽  
Shock Proteins

At least four proteins of 70,000 to 75,000 molecular weight (70-75K) were synthesized from mRNA which hybridized with a cloned heat shock gene previously shown to be localized to the 87A and 87C heat shock puff sites. These in vitro-synthesized proteins were indistinguishable from in vivo-synthesized heat shock-induced proteins when analyzed on sodium dodecyl sulfate-polyacrylamide gels. A comparison of the pattern of this group of proteins synthesized in vivo during a 5-min pulse or during continuous labeling indicates that the 72-75K proteins are probably not kinetic precursors to the major 70K heat shock protein. Partial digestion products generated with V8 protease indicated that the 70-75K heat shock proteins are closely related, but that there are clear differences between them. The partial digestion patterns obtained from heat shock proteins from the Kc cell line and from the Oregon R strain of Drosophila melanogaster are very similar. Genetic analysis of the patterns of 70-75K heat shock protein synthesis indicated that the genes encoding at least two of the three 72-75K heat shock proteins are located outside of the major 87A and 87C puff sites.

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