Changes in rates of synthesis of individual proteins in a psychrophilic bacterium after a shift in temperature

1991 ◽  
Vol 37 (11) ◽  
pp. 840-847 ◽  
Author(s):  
Tadashi Araki
Keyword(s):  
Steady State ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cold Shock ◽  
State Level ◽  
Psychrophilic Bacterium ◽  
Steady State Level ◽  
C Cells ◽  
State Growth ◽  
Shock Proteins

In the psychrophilic bacterium Vibrio sp. strain ANT-300, which has the ability to grow efficiently between 13 and −2 °C, with an optimum at 7 °C, cells in steady-state growth at 0 and 13 °C appeared to exhibit different patterns in the levels of certain individual proteins. With a shift in temperature, the steady-state level of individual proteins was achieved only after dramatic transient changes in the rates of synthesis of a small number of those proteins whose levels would be adjusted. Upon a shift up from 0 to 13 °C, the rates of synthesis of at least 25 proteins increased transiently, while increased rates of synthesis of 39 proteins were induced immediately upon a shift down from 13 to 0 °C. The proteins of which the levels would be adjusted were synthesized at differential rates, which varied conspicuously with respect to timing after the shifts in temperature. Such changes appear to be active regulatory responses to changes in temperature. Key words: psychrophile, Vibrio sp. strain ANT-300, heat-shock proteins, cold-shock proteins.

The effects of cold-temperature stress on gene expression in maize

1987 ◽  
Vol 65 (2) ◽  
pp. 112-119 ◽  
Author(s):  
Reza K. Yacoob ◽  
W. Gary Filion
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cold Shock ◽  
Incubation Temperature ◽  
Polyclonal Antibodies ◽  
Cold Shock Response ◽  
Shock Response ◽  
Acclimation Response ◽  
Molecular Masses ◽  
Shock Proteins

A rapid decrease from the 28 °C incubation temperature of 5-day-old maize seedlings induced a response recorded as an altered synthesis of several polypeptides. The maximum response occurred at 4 °C and included cold-shock proteins with relative molecular masses of 94, 92, 90, 73, 70, 54, 50, 44, 38, 34, 33, 32, 24, 20, and 14 kilodaltons (kDa). Western bolt analysis (probed with polyclonal antibodies against maize heat-shock proteins) and fluorograms prepared from one-dimensional gel electrophoresis of maize heat-shock proteins revealed differences between the cold-induced polypeptides and the maize heat-shock proteins. The abundance of low molecular weight polypeptides and the absence of a marked depression in normal protein synthesis were the most noted differences from the heat-shock response. The cold-shock response, which was induced by as little as a 3 °C reduction in temperature, showed some transitory proteins, was separate from an acclimation response, and lasted up to 18 h (after returning the seedlings to 28 °C) before the normal protein synthetic pattern returned. Seedlings allowed to recover from a 4 °C shock for 4 h at 28 °C showed synthesis of a 250-kDa polypeptide, which lasted less than 2 h and was completely inhibited by actinomycin D.

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 High constitutive levels of heat-shock proteins in human-pathogenic parasites of the genus Leishmania

1995 ◽  
Vol 310 (1) ◽  
pp. 225-232 ◽  
Author(s):  
S Brandau ◽  
A Dresel ◽  
J Clos
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
State Level ◽  
Protozoan Parasite ◽  
Cellular Stress Response ◽  
Transcriptional Level ◽  
Heat Shock Genes ◽  
Leishmania Promastigotes ◽  
Shock Proteins

We have analysed the transcription of three heat-shock genes, HSP70, HSP83 and ClpB, in the protozoan parasite Leishmania. All three heat-shock genes are transcribed constitutively and not heat-inducibly. However, we find that two major heat-shock proteins, HSP70 and HSP83, are synthesized at elevated rates during heat stress. We conclude that the cellular stress response in Leishmaniae is regulated exclusively on a post-transcriptional level much in contrast with all other eukaryotes examined so far. The induced synthesis of HSP70 and HSP83, however, does not increase the steady-state level of either protein significantly. This is compensated by high constitutive levels of both proteins: HSP70 and HSP83 make up 2.1% and 2.8%, respectively, of the total protein in unstressed Leishmania promastigotes. Also, HSP70 is a strictly cytoplasmic protein in Leishmania and does not relocate into the nucleus during heat stress, as it does in other eukaryotes examined in the past.

Heat shock proteins in willow (Salix viminalis)

1990 ◽  
Vol 80 (2) ◽  
pp. 301-306
Author(s):  
Tiina Vahala ◽  
Tage Eriksson ◽  
Peter Engstrom
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Salix Viminalis ◽  
Shock Proteins
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