Faculty Opinions recommendation of Adaptation of Bacillus subtilis to growth at low temperature: a combined transcriptomic and proteomic appraisal.

Author(s):  
Charles Dorman
Microbiology ◽  
2006 ◽  
Vol 152 (3) ◽  
pp. 831-853 ◽  
Author(s):  
Ina Budde ◽  
Leif Steil ◽  
Christian Scharf ◽  
Uwe Völker ◽  
Erhard Bremer

The soil bacterium Bacillus subtilis frequently encounters a reduction in temperature in its natural habitats. Here, a combined transcriptomic and proteomic approach has been used to analyse the adaptational responses of B. subtilis to low temperature. Propagation of B. subtilis in minimal medium at 15 °C triggered the induction of 279 genes and the repression of 301 genes in comparison to cells grown at 37 °C. The analysis thus revealed profound adjustments in the overall gene expression profile in chill-adapted cells. Important transcriptional changes in low-temperature-grown cells comprise the induction of the SigB-controlled general stress regulon, the induction of parts of the early sporulation regulons (SigF, SigE and SigG) and the induction of a regulatory circuit (RapA/PhrA and Opp) that is involved in the fine-tuning of the phosphorylation status of the Spo0A response regulator. The analysis of chill-stress-repressed genes revealed reductions in major catabolic (glycolysis, oxidative phosphorylation, ATP synthesis) and anabolic routes (biosynthesis of purines, pyrimidines, haem and fatty acids) that likely reflect the slower growth rates at low temperature. Low-temperature repression of part of the SigW regulon and of many genes with predicted functions in chemotaxis and motility was also noted. The proteome analysis of chill-adapted cells indicates a major contribution of post-transcriptional regulation phenomena in adaptation to low temperature. Comparative analysis of the previously reported transcriptional responses of cold-shocked B. subtilis cells with this data revealed that cold shock and growth in the cold constitute physiologically distinct phases of the adaptation of B. subtilis to low temperature.


1991 ◽  
Vol 71 (4) ◽  
pp. 281-283 ◽  
Author(s):  
Ancharida Svarachorn ◽  
Tetsuaki Tsuchido ◽  
Atsuhiko Shinmyo ◽  
Mitsuo Takano

2019 ◽  
Vol 95 (6) ◽  
pp. 588-592 ◽  
Author(s):  
V. A. Kolesnikov ◽  
Roman Yakushin ◽  
V. A. Brodsky ◽  
E. S. Babusenko ◽  
A. V. Chistolinov

There was investigated the effect of barrier and spark discharge low temperature plasma on water containing the cells of Escherichia coli (Escherichia coli), hay bacillus (Bacillus subtilis) and yeast (Saccharomyces cerevisiae). There was shown a general decline in the concentration of viable microbial cells after the treatment of suspensions. There was especially marked the detrimental effect of the method on the viability of sanitary-indicative coliform bacteria in the water.


2021 ◽  
Vol 18 ◽  
Author(s):  
Yan Shan ◽  
Junjie Shang ◽  
Dongfang Zhang ◽  
Yinshan Cui ◽  
Yi Wang ◽  
...  

Background: Amylase used in the market is mostly medium-temperature enzyme or high-temperature enzyme and has poor enzyme activity under low-temperature environment. Acid α-amylase can be used to develop digestion additives in the pharmaceutical and healthcare industries. The amino acid sequence and structural differences among α-amylases obtained from various organisms are high enough to confer interesting biochemical diversity to the enzymes. However, low- temperature (0-50℃) amylase, with an optimum temperature and heat sensitivity, has a greater potential value than medium (50-80℃) and high (80-110℃) temperature amylases. Methodology: The gene amy48 from encoding extracellular α-amylase in Bacillus subtilis YX48 was successfully cloned into the pET30a (+) vector and expressed in Escherichia coli BL21 (DE3) for biochemical characterization. Results and Conclusion: The molecular weight of α-amylase was 75 kDa. The activity of α-amylase was not affected by Ca2+, and Amy48 had the best activity at pH 5.0 and 37℃. AMY48 has high stability over a narrow pH and temperature range (5.0-8.0 and 30-45℃). Amylase activity was strongly inhibited by Zn2+, Mn2+, Cu2+, and Fe2+ ions, but Na+, K+, and Co2+ ions stimulate its activity slightly. The purified enzyme showed gradually reduced activity in the presence of detergents. However, it was remarkably stable against EDTA and urea.


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