Stress or heat shock protein synthesis and cellular filamentation in psychrophilic and psychrotrophic bacteria

1989 ◽  
Vol 152 (2) ◽  
pp. 148-153 ◽  
Author(s):  
Kirk L. McCallum ◽  
Barbara J. Butler ◽  
William E. Inniss
Keyword(s):  
Protein Synthesis ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Psychrotrophic Bacteria

scholarly journals Ribosome Profiling Reveals HSP90 Inhibitor Effects on Stage-Specific Protein Synthesis in Leishmania donovani

mSystems ◽  
2018 ◽  
Vol 3 (6) ◽  
Author(s):  
Eugenia Bifeld ◽  
Stephan Lorenzen ◽  
Katharina Bartsch ◽  
Juan-José Vasquez ◽  
T. Nicolai Siegel ◽  
...  
Keyword(s):  
Gene Expression ◽  
Protein Synthesis ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Leishmania Donovani ◽  
Specific Protein ◽  
Ribosome Profiling ◽  
Severe Illness ◽  
Content Type ◽  
Hsp90 Activity

ABSTRACT The 90-kDa heat shock protein (HSP90) of eukaryotes is a highly abundant and essential chaperone required for the maturation of regulatory and signal proteins. In the protozoan parasite Leishmania donovani, causative agent of the fatal visceral leishmaniasis, HSP90 activity is essential for cell proliferation and survival. Even more importantly, its inhibition causes life cycle progression from the insect stage to the pathogenic, mammalian stage. To unravel the molecular impact of HSP90 activity on the parasites’ gene expression, we performed a ribosome profiling analysis of L. donovani, comparing genome-wide protein synthesis patterns in the presence and absence of the HSP90-specific inhibitor radicicol and an ectopically expressed radicicol-resistant HSP90 variant. We find that ribosome-protected RNA faithfully maps open reading frames and represents 97% of the annotated protein-coding genes of L. donovani. Protein synthesis was found to correlate poorly with RNA steady-state levels, indicating a regulated translation as primary mechanism for HSP90-dependent gene expression. The results confirm inhibitory effects of HSP90 on the synthesis of Leishmania proteins that are associated with the pathogenic, intracellular stage of the parasite. Those include heat shock proteins, redox enzymes, virulence-enhancing surface proteins, proteolytic pathways, and a complete set of histones. Conversely, HSP90 promotes fatty acid synthesis enzymes. Complementing radicicol treatment with the radicicol-resistant HSP90rr variant revealed important off-target radicicol effects that control a large number of the above-listed proteins. Leishmania lacks gene-specific transcription regulation and relies on regulated translation instead. Our ribosome footprinting analysis demonstrates a controlling function of HSP90 in stage-specific protein synthesis but also significant, HSP90-independent effects of the inhibitor radicicol. IMPORTANCE Leishmania parasites cause severe illness in humans and animals. They exist in two developmental stages, insect form and mammalian form, which differ in shape and gene expression. By mapping and quantifying RNA fragments protected by protein synthesis complexes, we determined the rates of protein synthesis for >90% of all Leishmania proteins in response to the inhibition of a key regulatory protein, the 90-kDa heat shock protein. We find that Leishmania depends on a regulation of protein synthesis for controlling its gene expression and that heat shock protein 90 inhibition can trigger the developmental program from insect form to mammalian form of the pathogen.

Thermosensitization, heat shock protein synthesis and development of thermotolerance in M-14 human tumor cells subjected to step-down heating

1992 ◽  
Vol 31 (4) ◽  
pp. 323-332 ◽  
Author(s):  
Andrea Delpino ◽  
Francesco Paolo Gentile ◽  
Francesca Di Modugno ◽  
Marcello Benassi ◽  
Anna Maria Mileo ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Tumor Cells ◽  
Human Tumor ◽  
Human Tumor Cells ◽  
Step Down ◽  
M 14

Adenovirus E1A requires synthesis of a cellular protein to establish a stable transcription complex in injected Xenopus laevis oocytes

1987 ◽  
Vol 7 (9) ◽  
pp. 3049-3056
Author(s):  
J D Richter ◽  
H C Hurst ◽  
N C Jones
Keyword(s):  
Protein Synthesis ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Mammalian Cells ◽  
Cellular Protein ◽  
Xenopus Laevis Oocytes ◽  
Protein Synthesis Inhibitors ◽  
Adenovirus E1a ◽  
High Level

The Escherichia coli-expressed adenovirus E1A 13S mRNA product injected into Xenopus oocytes was active, as assessed by its ability to stimulate the transcription of an injected gene which is normally responsive to E1A in mammalian cells. In the presence of the protein synthesis inhibitors pactamycin or cycloheximide, E1A was correctly posttranslationally modified (phosphorylated) and transported to the nucleus; but it failed to stimulate the transcription of an injected gene containing the human heat shock protein 70 promoter. The basal (unstimulated) level of transcription of the gene was unaffected by these inhibitors. If oocytes were cultured in the presence of cycloheximide after E1A stimulated transcription, however, the high level of transcription was maintained for several hours without new protein synthesis. Results of competition studies with the same promoter (the heat shock protein 70 promoter) linked to two marked genes demonstrated that once the induction of transcription by E1A took place, the stimulated levels of transcription were maintained, even when they were challenged with excess competitor DNA. Results of these studies suggest that E1A requires the synthesis of a cellular protein to form a stable transcription complex.

scholarly journals Dinitrosyl iron complexes with thiol-containing ligands and S -nitroso-D,L -penicillamine as inductors of heat shock protein synthesis in H35 hepatoma cells

FEBS Letters ◽  
1999 ◽  
Vol 455 (1-2) ◽  
pp. 179-182 ◽  
Author(s):  
Frederik A.C. Wiegant ◽  
Igor Y. Malyshev ◽  
Andrey L. Kleschyov ◽  
Ernst van Faassen ◽  
Anatoly F. Vanin
Keyword(s):  
Protein Synthesis ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Iron Complexes ◽  
Hepatoma Cells ◽  
Dinitrosyl Iron Complexes ◽  
Dinitrosyl Iron

Genetic Diversity of Heat Shock Protein Synthesis in Cereal Plants

1989 ◽  
pp. 319-330 ◽  
Author(s):  
H. T. Nguyen ◽  
M. Krishnan ◽  
J. J. Burke ◽  
R. D. Porter ◽  
R. A. Vierling
Keyword(s):  
Genetic Diversity ◽  
Protein Synthesis ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cereal Plants

scholarly journals Heat-shock protein synthesis in cotton is cultivar dependent

1993 ◽  
Vol 10 (2) ◽  
pp. 95-97 ◽  
Author(s):  
J. A. de Ronde ◽  
A. van der Mescht ◽  
W. A. Cress
Keyword(s):  
Protein Synthesis ◽  
Heat Shock ◽  
Heat Shock Protein
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