Cold shock proteins and cold acclimation proteins in the psychrotrophic bacteriumPseudomonas putidaQ5 and its transconjugant

1996 ◽  
Vol 42 (8) ◽  
pp. 798-803 ◽  
Author(s):  
Andrew W. Gumley ◽  
William E. Inniss
Keyword(s):  
Cold Acclimation ◽  
Cold Shock ◽  
Additional Stress ◽  
Tol Plasmid ◽  
Two Dimensional Gel Electrophoresis ◽  
Cold Shock Proteins ◽  
Psychrotrophic Bacterium ◽  
Shock Proteins ◽  
Similar Growth ◽  
Constant Growth

The production of cold shock proteins (csps) and cold acclimation proteins (caps) was characterized in the psychrotrophic bacterium Pseudomonas putida Q5 and its transconjugant P. putida Q5T which contains the toluene-degradative TOL (pWWO) plasmid, using two-dimensional gel electrophoresis and computing scanning laser densitometry. Similar growth rates for the psychrotrophic bacterium P. putida Q5 and the transconjugant were found at temperatures ranging from 30 to 0 °C. Sixteen proteins were quantified and compared in P. putida Q5 and P. putida Q5T following a 25 to 5 °C cold shock or constant growth at 5 °C. During constant growth at 25 °C, a decrease in the synthesis of various proteins occurred in the transconjugant. Following cold shock to 5 °C or constant growth at 5 °C, csps and caps were produced with a greater number occurring in the transconjugant. This may suggest an additional stress response in the transconjugant owing to metabolic load exerted by the TOL plasmid. Growth of P. putida Q5T with toluate produced seven proteins that appeared to be TOL-plasmid mediated and of which some were also designated as caps.Key words: cold shock proteins, cold acclimation proteins, TOL pWWO plasmid, psychrotrophic bacterium.

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 Adaptation to Cold and Proteomic Responses of the Psychrotrophic Biopreservative Lactococcus piscium Strain CNCM I-4031

2010 ◽  
Vol 76 (24) ◽  
pp. 8011-8018 ◽  
Author(s):  
Matthieu Garnier ◽  
Sebastien Matamoros ◽  
Didier Chevret ◽  
Marie-France Pilet ◽  
Francoise Leroi ◽  
...  
Keyword(s):  
Cold Acclimation ◽  
Stress Responses ◽  
Cold Adaptation ◽  
Cold Shock ◽  
Two Dimensional Gel Electrophoresis ◽  
Psychrotrophic Bacteria ◽  
Liquid Chromatography Tandem Mass ◽  
Shock Proteins ◽  
Proteomic Responses ◽  
Oxidative Stress Responses

ABSTRACT There is considerable interest in the use of psychrotrophic bacteria for food biopreservation and in the understanding of cold adaptation mechanisms. The psychrotrophic biopreservative Lactococcus piscium strain CNCM I-4031 was studied for its growth behavior and proteomic responses after cold shock and during cold acclimation. Growth kinetics highlighted the absence of growth latency after cold shock, suggesting a very high promptness in cold adaptation, a behavior that has never been described before for lactic acid bacteria (LAB). A comparative proteomic analysis was applied with two-dimensional gel electrophoresis (2-DE), and upregulated proteins were identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS). Both cold shock and cold acclimation triggered the upregulation of proteins involved in general and oxidative stress responses and fatty acid and energetic metabolism. However, 2-DE profiles and upregulated proteins were different under both conditions, suggesting a sequence of steps in cold adaptation. In addition, the major 7-kDa Csp protein was identified in the L. piscium CNCM I-4031 genome but was not cold regulated. The implication of the identified cold shock proteins and cold acclimation proteins in efficient cold adaptation, the possible regulation of a histidyl phosphocarrier protein, and the roles of a constitutive major 7-kDa Csp are discussed.

scholarly journals Physiological and Regulatory Effects of Controlled Overproduction of Five Cold Shock Proteins of Lactococcus lactisMG1363

2000 ◽  
Vol 66 (9) ◽  
pp. 3756-3763 ◽  
Author(s):  
Jeroen A. Wouters ◽  
Marielle Mailhes ◽  
Frank M. Rombouts ◽  
Willem M. de Vos ◽  
Oscar P. Kuipers ◽  
...  
Keyword(s):  
Total Protein ◽  
Northern Blot Analysis ◽  
Cold Shock ◽  
Two Dimensional Gel Electrophoresis ◽  
Cold Shock Proteins ◽  
Regulatory Effects ◽  
Rna Stabilization ◽  
The Stability ◽  
Shock Proteins ◽  
Induced Proteins

ABSTRACT The physiological and regulatory effects of overproduction of five cold shock proteins (CSPs) of Lactococcus lactis were studied. CspB, CspD, and CspE could be overproduced at high levels (up to 19% of the total protein), whereas for CspA and CspC limited overproduction (0.3 to 0.5% of the total protein) was obtained. Northern blot analysis revealed low abundance of the cspCtranscript, indicating that the stability of cspC mRNA is low. The limited overproduction of CspA is likely to be caused by low stability of CspA since when there was an Arg-Pro mutation at position 58, the level of CspA production increased. Using two-dimensional gel electrophoresis, it was found that upon overproduction of the CSPs several proteins, including a number of cold-induced proteins ofL. lactis, were induced. Strikingly, upon overproduction of CspC induction of CspB, putative CspF, and putative CspG was also observed. Overproduction of CspB and overproduction of CspE result in increased survival when L. lactis is frozen (maximum increases, 10- and 5-fold, respectively, after 4 freeze-thaw cycles). It is concluded that in L. lactis CSPs play a regulatory role in the cascade of events that are initiated by cold shock treatment and that they either have a direct protective effect during freezing (e.g., RNA stabilization) or induce other factors involved in the freeze-adaptive response or both.

scholarly journals Cold Shock Proteins and Low-Temperature Response ofStreptococcus thermophilus CNRZ302

1999 ◽  
Vol 65 (10) ◽  
pp. 4436-4442 ◽  
Author(s):  
Jeroen A. Wouters ◽  
Frank M. Rombouts ◽  
Willem M. de Vos ◽  
Oscar P. Kuipers ◽  
Tjakko Abee
Keyword(s):  
Low Temperature ◽  
Cold Shock ◽  
Thermophilic Bacterium ◽  
Temperature Adaptation ◽  
Transcriptional Level ◽  
Minimal Growth ◽  
Two Dimensional Gel Electrophoresis ◽  
Cold Shock Proteins ◽  
Shock Proteins ◽  
Induced Proteins

ABSTRACT Low-temperature adaptation and cryoprotection were studied in the thermophilic lactic acid bacterium Streptococcus thermophilus CNRZ302. S. thermophilus actively adapts to freezing during a pretreatment at 20°C, resulting in an approximately 1,000-fold increased survival after four freeze-thaw cycles compared to mid-exponential-phase cells grown at an optimal temperature of 42°C. No adaptation is observed when cells are exposed to a temperature (10°C) below the minimal growth temperature of the strain (just below 15°C). By two-dimensional gel electrophoresis several 7-kDa cold-induced proteins were identified, which are the major induced proteins after a shift to 20°C. These cold shock proteins were maximally expressed at 20°C, while the induction level was low after cold shock to 10°C. To confirm the presence ofcsp genes in S. thermophilus, a PCR strategy was used which yielded products of different sizes. Sequence analysis revealed csp-like sequences that were up to 95% identical to those of csp genes of S. thermophilus ST1-1,Streptococcus dysgalactiae, Streptococcus pyogenes, and Lactococcus lactis. Northern blot analysis revealed a seven- to ninefold induction of cspmRNA after a temperature shift to 20°C, showing that this thermophilic bacterium indeed contains at least one cold-induciblecsp gene and that its regulation takes place at the transcriptional level.

Expression of Major Cold Shock Proteins and Genes by Yersinia enterocolitica in Synthetic Medium and Foods

2005 ◽  
Vol 68 (11) ◽  
pp. 2454-2458 ◽  
Author(s):  
THIRUNAVUKKARASU ANNAMALAI ◽  
KUMAR VENKITANARAYANAN
Keyword(s):  
Yersinia Enterocolitica ◽  
Cold Shock ◽  
Synthetic Medium ◽  
Foodborne Pathogen ◽  
Skim Milk ◽  
Luria Bertani ◽  
Dot Blot ◽  
Two Dimensional Gel Electrophoresis ◽  
Cold Shock Proteins ◽  
Shock Proteins

Yersinia enterocolitica is a psychrotrophic foodborne pathogen that has been implicated in outbreaks of foodborne illness involving cold-stored foods, especially milk and pork. A major mechanism bacteria use to adapt to cold is expression of cold shock proteins. The objective of this research was to study the expression of major cold shock proteins of Y. enterocolitica in Luria-Bertani (LB) broth, milk, and pork following a temperature downshift from 30 to 4°C. Y. enterocolitica was inoculated into 10 ml of LB broth, sterile skim milk, or pork, and the samples were stored at 4°C (cold shock) or 30°C (control) for 0, 4, 8, 12, and 24 h. At each sampling time, total protein and total RNA were extracted from Y. enterocolitica harvested from LB broth, milk, and pork and subjected to two-dimensional gel electrophoresis and dot blot analysis. Two major cold shock proteins (CspA1 and CspA2) of ∼7 kDa and their genes were expressed by Y. enterocolitica following cold shock. However, the CspA1 and CspA2 proteins were not expressed by Y. enterocolitica at 30°C. Y. enterocolitica CspA1 and CspA2 were observed as early as 2 h of cold shock in cultures from LB broth and milk and at 8 h of cold shock in cultures from pork.

scholarly journals Enhanced Levels of Cold Shock Proteins in Listeria monocytogenes LO28 upon Exposure to Low Temperature and High Hydrostatic Pressure

2002 ◽  
Vol 68 (2) ◽  
pp. 456-463 ◽  
Author(s):  
Henrike H. Wemekamp-Kamphuis ◽  
Andreas K. Karatzas ◽  
Jeroen A. Wouters ◽  
Tjakko Abee
Keyword(s):  
Listeria Monocytogenes ◽  
Hydrostatic Pressure ◽  
Low Temperature ◽  
High Hydrostatic Pressure ◽  
Cold Shock ◽  
Chromosomal Dna ◽  
Two Dimensional Gel Electrophoresis ◽  
Cold Shock Proteins ◽  
Food Borne ◽  
Shock Proteins

ABSTRACT Listeria monocytogenes is a psychrotrophic food-borne pathogen that is problematic for the food industry because of its ubiquitous distribution in nature and its ability to grow at low temperatures and in the presence of high salt concentrations. Here we demonstrate that the process of adaptation to low temperature after cold shock includes elevated levels of cold shock proteins (CSPs) and that the levels of CSPs are also elevated after treatment with high hydrostatic pressure (HHP). Two-dimensional gel electrophoresis combined with Western blotting performed with anti-CspB of Bacillus subtilis was used to identify four 7-kDa proteins, designated Csp1, Csp2, Csp3, and Csp4. In addition, Southern blotting revealed four chromosomal DNA fragments that reacted with a csp probe, which also indicated that a CSP family is present in L. monocytogenes LO28. After a cold shock in which the temperature was decreased from 37�C to 10�C the levels of Csp1 and Csp3 increased 10- and 3.5-fold, respectively, but the levels of Csp2 and Csp4 were not elevated. Pressurization of L. monocytogenes LO28 cells resulted in 3.5- and 2-fold increases in the levels of Csp1 and Csp2, respectively. Strikingly, the level of survival after pressurization of cold-shocked cells was 100-fold higher than that of cells growing exponentially at 37�C. These findings imply that cold-shocked cells are protected from HHP treatment, which may affect the efficiency of combined preservation techniques.

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.

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