scholarly journals Transcriptomic response of an Antarctic yeast Rhodotorula sp. USM-PSY62 to temperature changes

2020 ◽  
Author(s):  
Cleo-Nicole Chai ◽  
Hok-Chai Yam ◽  
Nurlina Rosli ◽  
Azali Azlan ◽  
Ghows Azzam ◽  
...  
Keyword(s):  
Heat Shock ◽  
Protein Transport ◽  
Cold Shock ◽  
Shock Condition ◽  
Transcriptomic Response ◽  
Dna And Rna ◽  
Antarctic Sea Ice ◽  
Magnesium Transporter ◽  
Heat Shock Responses ◽  
Enzyme Cofactors

AbstractRhodotorula sp. (USM-PSY62) is a psychrophilic yeast isolated from Antarctic sea ice and it grows optimally at 15 °C. This study was set up to observe how USM-PSY62 adapted to fluctuations in temperature. During cold adaptation, an elevated transcription of the CorA magnesium transporter gene in USM-PSY62 indicated a higher requirement for magnesium ions in order to gain additional enzyme cofactors or maintain cytoplasmic fluidity. The HepA homologue coding for DNA/RNA helicase was also over-expressed in cold condition possibly to reorganize secondary structures of DNA and RNA. An up-regulation of the catalase gene was also observed reflecting an increment in the concentration of reactive oxygen species and fluctuations in the associated antioxidant system. The YOP1 gene, which encodes a membrane protein associated with protein transport and membrane traffic, was the most down-regulated under cold shock condition. The genes responsible for the structural maintenance of chromosome (SMC) were also down-regulated when the temperature was shifted to 0 °C. Upon cold shock, the gene for heat shock factor protein 1 (HSF1) was also down-regulated. Hsf1 is a transcriptional regulator which regulate the heat shock responses. Although USM-PSY62 showed some common adaptive strategies as in several other psychrophilic organisms, new mechanisms were also uncovered.

scholarly journals Characterization of the Staphylococcus aureus Heat Shock, Cold Shock, Stringent, and SOS Responses and Their Effects on Log-Phase mRNA Turnover

2006 ◽  
Vol 188 (19) ◽  
pp. 6739-6756 ◽  
Author(s):  
Kelsi L. Anderson ◽  
Corbette Roberts ◽  
Terrence Disz ◽  
Veronika Vonstein ◽  
Kaitlyn Hwang ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Stress Response ◽  
Heat Shock ◽  
Stress Responses ◽  
Cold Shock ◽  
Rna Stability ◽  
Open Reading Frames ◽  
Mrna Turnover ◽  
Small Stable Rna ◽  
Heat Shock Responses

ABSTRACT Despite its being a leading cause of nosocomal and community-acquired infections, surprisingly little is known about Staphylococcus aureus stress responses. In the current study, Affymetrix S. aureus GeneChips were used to define transcriptome changes in response to cold shock, heat shock, stringent, and SOS response-inducing conditions. Additionally, the RNA turnover properties of each response were measured. Each stress response induced distinct biological processes, subsets of virulence factors, and antibiotic determinants. The results were validated by real-time PCR and stress-mediated changes in antimicrobial agent susceptibility. Collectively, many S. aureus stress-responsive functions are conserved across bacteria, whereas others are unique to the organism. Sets of small stable RNA molecules with no open reading frames were also components of each response. Induction of the stringent, cold shock, and heat shock responses dramatically stabilized most mRNA species. Correlations between mRNA turnover properties and transcript titers suggest that S. aureus stress response-dependent alterations in transcript abundances can, in part, be attributed to alterations in RNA stability. This phenomenon was not observed within SOS-responsive cells.

Ubiquitin gene expression in Dictyostelium is induced by heat and cold shock, cadmium, and inhibitors of protein synthesis

1988 ◽  
Vol 90 (1) ◽  
pp. 51-58 ◽  
Author(s):  
A. Muller-Taubenberger ◽  
J. Hagmann ◽  
A. Noegel ◽  
G. Gerisch
Keyword(s):  
Gene Expression ◽  
Protein Synthesis ◽  
Heat Shock ◽  
Differential Expression ◽  
Dictyostelium Discoideum ◽  
Heat Shock Response ◽  
Cold Shock ◽  
Multifunctional Protein ◽  
Cadmium Treatment ◽  
Shock Response

Ubiquitin is a highly conserved, multifunctional protein, which is implicated in the heat-shock response of eukaryotes. The differential expression of the multiple ubiquitin genes in Dictyostelium discoideum was investigated under various stress conditions. Growing D. discoideum cells express four major ubiquitin transcripts of sizes varying from 0.6 to 1.9 kb. Upon heat shock three additional ubiquitin mRNAs of 0.9, 1.2 and 1.4 kb accumulate within 30 min. The same three transcripts are expressed in response to cold shock or cadmium treatment. Inhibition of protein synthesis by cycloheximide leads to a particularly strong accumulation of the larger ubiquitin transcripts, which code for polyubiquitins. Possible mechanisms regulating the expression of ubiquitin transcripts upon heat shock and other stresses are discussed.

Increased production of genetic mosaics in Habrobracon juglandis by cold shock of newly oviposited eggs

Development ◽  
1976 ◽  
Vol 36 (1) ◽  
pp. 127-131
Author(s):  
R. M. Petters ◽  
D. S. Grosch
Keyword(s):  
Heat Shock ◽  
Cold Shock ◽  
Differential Mortality ◽  
Wild Type ◽  
Cleavage Stage ◽  
Genetic Mosaics

Eggs from an ebony stock exposed to 5·5°C prior to syngamy exhibited increased production of genetic mosaics in comparison with untreated eggs from the same females. No increase in mosaic production occurred for cold-shocked cleavage-stage embryos from the ebony stock or from pre-cleavage cold-shocked eggs from a wild-type stock. Heat shock of pre-syngamy eggs also failed to increase the production of genetic mosaics. These findings are onsistent with predictions based on the post-cleavage fertilization theory of mosaic origin in Habrobracon or with a hypothesis of differential mortality.

A developmentally regulated membrane protein gene in Dictyostelium discoideum is also induced by heat shock and cold shock

1988 ◽  
Vol 8 (1) ◽  
pp. 153-159
Author(s):  
M Maniak ◽  
W Nellen
Keyword(s):  
Heat Shock ◽  
Membrane Protein ◽  
Rna Processing ◽  
Cold Shock ◽  
Protein Gene ◽  
Nuclear Accumulation ◽  
Control Mechanisms ◽  
Developmentally Regulated ◽  
Hydrophobic Peptide ◽  
Membrane Protein Gene

We have analyzed the expression of the Dictyostelium gene P8A7 which had been isolated as a cDNA clone from an early developmentally regulated gene. The single genomic copy generated two mRNAs which were subject to different control mechanisms: while one mRNA (P8A7S) was regulated like the cell-type-nonspecific late genes, the other one (P8A7L) was induced during development, when cells were allowed to attach to a substrate, and when cells were subjected to stress, such as heat shock and cadmium. Interestingly the same induction was also observed with cold shock. RNA processing was inhibited by heat and cold shock, leading to nuclear accumulation of a precursor. The translated region of the cDNA was common to both mRNAs and encoded an unusually hydrophobic peptide with the characteristics of a membrane protein.

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.

Heat shock but not cold shock leads to disturbed intracellular zinc homeostasis

2009 ◽  
pp. n/a-n/a ◽  
Author(s):  
Elvis Pirev ◽  
Yasemin Ince ◽  
Helmut Sies ◽  
Klaus D. Kröncke
Keyword(s):  
Heat Shock ◽  
Cold Shock ◽  
Zinc Homeostasis ◽  
Intracellular Zinc

scholarly journals A developmentally regulated membrane protein gene in Dictyostelium discoideum is also induced by heat shock and cold shock.

1988 ◽  
Vol 8 (1) ◽  
pp. 153-159 ◽  
Author(s):  
M Maniak ◽  
W Nellen
Keyword(s):  
Heat Shock ◽  
Membrane Protein ◽  
Rna Processing ◽  
Cold Shock ◽  
Protein Gene ◽  
Nuclear Accumulation ◽  
Control Mechanisms ◽  
Developmentally Regulated ◽  
Hydrophobic Peptide ◽  
Membrane Protein Gene

We have analyzed the expression of the Dictyostelium gene P8A7 which had been isolated as a cDNA clone from an early developmentally regulated gene. The single genomic copy generated two mRNAs which were subject to different control mechanisms: while one mRNA (P8A7S) was regulated like the cell-type-nonspecific late genes, the other one (P8A7L) was induced during development, when cells were allowed to attach to a substrate, and when cells were subjected to stress, such as heat shock and cadmium. Interestingly the same induction was also observed with cold shock. RNA processing was inhibited by heat and cold shock, leading to nuclear accumulation of a precursor. The translated region of the cDNA was common to both mRNAs and encoded an unusually hydrophobic peptide with the characteristics of a membrane protein.

scholarly journals A large decrease in heat-shock-induced proteolysis after tryptophan starvation leads to increased expression of phage λ lysozyme cloned in Escherichia coli

1992 ◽  
Vol 286 (1) ◽  
pp. 187-191 ◽  
Author(s):  
P Soumillion ◽  
J Fastrez
Keyword(s):  
Escherichia Coli ◽  
Heat Shock ◽  
Stationary Phase ◽  
Coli Strain ◽  
Present Knowledge ◽  
R Gene ◽  
Gene Coding ◽  
Heat Shock Responses ◽  
Multicopy Vector ◽  
Thermal Induction

The R gene coding for phage lambda lysozyme (lambda L), cloned under the control of the PL promoter on a multicopy vector, is expressed in an Escherichia coli strain auxotrophic for tryptophan. Induction by a thermal shift after tryptophan supplementation in a culture initially brought into stationary phase by tryptophan starvation leads to highly increased expression. A thermally unstable mutant protein, difficult to obtain under standard conditions, can be easily produced by post-stationary-phase expression. It is shown that this is due to a drastic decrease in the heat-shock-induced proteolysis normally observed on thermal induction. These data are discussed in relation to our present knowledge of stringent and heat-shock responses.

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