Induction of protein synthesis in response to cold shock in the psychrotrophic yeast Trichosporon pullulans

1990 ◽  
Vol 36 (8) ◽  
pp. 519-524 ◽  
Author(s):  
Craig R. Julseth ◽  
William E. Inniss
Keyword(s):  
Cold Shock ◽  
Electrophoretic Analysis ◽  
Two Dimensional ◽  
Optimum Growth ◽  
Cold Shock Proteins ◽  
Optimum Growth Temperature ◽  
Maximum Induction ◽  
Shock Proteins ◽  
Key Words Cold Shock ◽  
Key Words Cold

The synthesis of proteins in response to a cold shock in the psychrotrophic yeast Trichosporon pullulans was examined. Two-dimensional electrophoretic analysis of a 21 to 5 °C cold shock revealed the induction of 26 cold-shock proteins (csps) at the maximum induction time of 12 h. The induction of only 10 csps after a 24 to 5 °C cold shock suggested that the growth of cells above their optimum growth temperature reduced their ability to induce csps. Comparison of the csp profile obtained after a 15 to a 5 °C cold shock with the profile for the 21 to 5 °C cold shock suggested that the range of the cold shock influences which proteins are induced. Key words: cold-shock proteins, psychrotrophic yeast.

Cold shock proteins and cold acclimation proteins in a psychrotrophic bacterium

1992 ◽  
Vol 38 (12) ◽  
pp. 1281-1285 ◽  
Author(s):  
Lyle G. Whyte ◽  
William E. Inniss
Keyword(s):  
Cold Acclimation ◽  
Cold Shock ◽  
Continuous Growth ◽  
Cold Shock Proteins ◽  
Psychrotrophic Bacterium ◽  
Cold Sensitive ◽  
Molecular Masses ◽  
Bacterium Bacillus ◽  
Shock Proteins ◽  
Key Words Cold Shock

The synthesis of proteins in the psychrotrophic bacterium Bacillus psychrophilus in response to both cold shock and continuous growth at low temperatures was examined. Cold shocks of 20 to 0, 5, or 10 °C resulted in the induction of nine, seven, and five cold shock proteins, respectively, as determined by 2-dimensional gel electrophoresis and computing scanning laser densitometry. Two cold shock proteins, with molecular masses of 61 and 34 kDa, which were induced in B. psychrophilus by cold shocks of 20 to 0 or 5 °C, were not induced in a cold-sensitive mutant of B. psychrophilus. Analysis of protein profiles of B. psychrophilus during continuous growth at 0, 5, or 10 °C revealed the synthesis of 11, 10, and 4 cold acclimation proteins, respectively. Some of these cold acclimation proteins were similar to cold shock proteins. In addition, the relative synthesis of both cold shock proteins and cold acclimation proteins increased with decreasing temperature. Thus, both types of proteins increased both in number and relative synthesis in response to cold shock and continuous growth at low temperature. Key words: cold shock proteins, cold acclimation proteins, psychrotrophic bacterium.

scholarly journals Listeria monocytogenes Cold Shock Proteins: Small Proteins with A Huge Impact

2021 ◽  
Vol 9 (5) ◽  
pp. 1061
Author(s):  
Francis Muchaamba ◽  
Roger Stephan ◽  
Taurai Tasara
Keyword(s):  
Listeria Monocytogenes ◽  
Stress Tolerance ◽  
Cold Shock ◽  
Current Data ◽  
Health Concern ◽  
Stress Exposure ◽  
Cold Shock Proteins ◽  
Cell Functions ◽  
Small Proteins ◽  
Shock Proteins

Listeria monocytogenes has evolved an extensive array of mechanisms for coping with stress and adapting to changing environmental conditions, ensuring its virulence phenotype expression. For this reason, L. monocytogenes has been identified as a significant food safety and public health concern. Among these adaptation systems are cold shock proteins (Csps), which facilitate rapid response to stress exposure. L. monocytogenes has three highly conserved csp genes, namely, cspA, cspB, and cspD. Using a series of csp deletion mutants, it has been shown that L. monocytogenes Csps are important for biofilm formation, motility, cold, osmotic, desiccation, and oxidative stress tolerance. Moreover, they are involved in overall virulence by impacting the expression of virulence-associated phenotypes, such as hemolysis and cell invasion. It is postulated that during stress exposure, Csps function to counteract harmful effects of stress, thereby preserving cell functions, such as DNA replication, transcription and translation, ensuring survival and growth of the cell. Interestingly, it seems that Csps might suppress tolerance to some stresses as their removal resulted in increased tolerance to stresses, such as desiccation for some strains. Differences in csp roles among strains from different genetic backgrounds are apparent for desiccation tolerance and biofilm production. Additionally, hierarchical trends for the different Csps and functional redundancies were observed on their influences on stress tolerance and virulence. Overall current data suggest that Csps have a wider role in bacteria physiology than previously assumed.

scholarly journals Cold Shock Proteins of Lactococcus lactis MG1363 Are Involved in Cryoprotection and in the Production of Cold-Induced Proteins

2001 ◽  
Vol 67 (11) ◽  
pp. 5171-5178 ◽  
Author(s):  
Jeroen A. Wouters ◽  
Hélène Frenkiel ◽  
Willem M. de Vos ◽  
Oscar P. Kuipers ◽  
Tjakko Abee
Keyword(s):  
Low Temperature ◽  
Lactococcus Lactis ◽  
Type Strain ◽  
Wild Type Strain ◽  
Cold Shock ◽  
Transcriptional Level ◽  
Wild Type ◽  
Cold Shock Proteins ◽  
Shock Proteins ◽  
Induced Proteins

ABSTRACT Members of the group of 7-kDa cold-shock proteins (CSPs) are the proteins with the highest level of induction upon cold shock in the lactic acid bacterium Lactococcus lactis MG1363. By using double-crossover recombination, two L. lactis strains were generated in which genes encoding CSPs are disrupted: L. lactis NZ9000ΔAB lacks the tandemly orientatedcspA and cspB genes, and NZ9000ΔABE lackscspA, cspB, and cspE. Both strains showed no differences in growth at normal and at low temperatures compared to that of the wild-type strain, L. lactis NZ9000. Two-dimensional gel electrophoresis showed that upon disruption of thecspAB genes, the production of remaining CspE at low temperature increased, and upon disruption of cspA, cspB, and cspE, the production of CspD at normal growth temperatures increased. Northern blot analysis showed that control is most likely at the transcriptional level. Furthermore, it was established by a proteomics approach that some (non-7-kDa) cold-induced proteins (CIPs) are not cold induced in the csp-lacking strains, among others the histon-like protein HslA and the signal transduction protein LlrC. This supports earlier observations (J. A. Wouters, M. Mailhes, F. M. Rombouts, W. M. De Vos, O. P. Kuipers, and T. Abee, Appl. Environ. Microbiol. 66:3756–3763, 2000). that the CSPs of L. lactis might be directly involved in the production of some CIPs upon low-temperature exposure. Remarkably, the adaptive response to freezing by prior exposure to 10°C was significantly reduced in strain NZ9000ΔABE but not in strain NZ9000ΔAB compared to results with wild-type strain NZ9000, indicating a notable involvement of CspE in cryoprotection.

scholarly journals RNA target profiles direct the discovery of virulence functions for the cold-shock proteins CspC and CspE

2017 ◽  
pp. 201620772 ◽  
Author(s):  
Charlotte Michaux ◽  
Erik Holmqvist ◽  
Erin Vasicek ◽  
Malvika Sharan ◽  
Lars Barquist ◽  
...  
Keyword(s):  
Cold Shock ◽  
Cold Shock Proteins ◽  
Shock Proteins

scholarly journals The Role of Electrostatics and Folding Kinetics on the Thermostability of Homologous Cold Shock Proteins

2020 ◽  
Vol 60 (2) ◽  
pp. 546-561 ◽  
Author(s):  
Paulo Henrique Borges Ferreira ◽  
Frederico Campos Freitas ◽  
Michelle E. McCully ◽  
Gabriel Gouvêa Slade ◽  
Ronaldo Junio de Oliveira
Keyword(s):  
Cold Shock ◽  
Folding Kinetics ◽  
Cold Shock Proteins ◽  
Shock Proteins

On Heat and Cells and Proteins

Physiology ◽  
2004 ◽  
Vol 19 (1) ◽  
pp. 11-15 ◽  
Author(s):  
Dörthe M. Katschinski
Keyword(s):  
Temperature Field ◽  
Heat Shock ◽  
Temperature Control ◽  
Cold Shock ◽  
Control Strategies ◽  
Cellular Function ◽  
The Body ◽  
Cold Shock Proteins ◽  
Shock Proteins

Two principal forms of temperature-control strategies have evolved, i.e., poikilothermic and homeothermic life. Even in homeothermic animals, the temperature field of the body is not homogenous. These observed temperature differences can affect cellular function directly or via the expression of heat shock or cold shock proteins.

scholarly journals Cold Shock Response and Major Cold Shock Proteins of Vibrio cholerae

2003 ◽  
Vol 69 (11) ◽  
pp. 6361-6369 ◽  
Author(s):  
Partha Pratim Datta ◽  
Rupak K. Bhadra
Keyword(s):  
Vibrio Cholerae ◽  
Cold Shock ◽  
De Novo ◽  
Alternative Pathway ◽  
Regulation Of Gene Expression ◽  
Inducible Promoter ◽  
Small Chromosome ◽  
Cold Shock Proteins ◽  
Shock Proteins ◽  
Kinetics Of

ABSTRACT When exponentially growing Vibrio cholerae cells were shifted from 37°C to various lower temperatures, it was found that the organism could adapt and grow at temperatures down to 15°C, below which the growth was completely arrested. There was no difference between the patterns of the cold shock responses in toxinogenic and nontoxinogenic strains of V. cholerae. Gel electrophoretic analyses of proteins of cold-exposed cells revealed significant induction of two major cold shock proteins (Csps), whose molecular masses were 7.7 kDa (CspAVC) and 7.5 kDa (CspV), and six other Csps, most of which were much larger. We cloned, sequenced, and analyzed the cspV gene encoding the CspV protein of V. cholerae O139 strain SG24. Although CspAVC and CspV have similar kinetics of synthesis and down-regulation, the corresponding genes, cspA and cspV, which are located in the small chromosome, are not located in the same operon. A comparative analysis of the kinetics of synthesis revealed that the CspV protein was synthesized de novo only during cold shock. Although both CspAVC and CspV were stable for several hours in the cold, the CspV protein was degraded rapidly when the culture was shifted back to 37°C, suggesting that this protein is probably necessary for adaptation at lower temperatures. Northern blot analysis confirmed that the cspV gene is cold shock inducible and is regulated tightly at the level of transcription. Interestingly, the cspV gene has a cold shock-inducible promoter which is only 12 nucleotides from the translational start site, and therefore, it appears that no unusually long 5′ untranslated region is present in its mRNA transcript. Thus, this promoter is an exception compared to other promoters of cold shock-inducible genes of different organisms, including Escherichia coli. Our results suggest that V. cholerae may use an alternative pathway for regulation of gene expression during cold shock.

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