Effect of different carbon sources and cold shock on protein synthesis by a psychrotrophicAcinetobactersp.

2002 ◽  
Vol 48 (3) ◽  
pp. 239-244 ◽  
Author(s):  
S E Barbaro ◽  
J T Trevors ◽  
W E Inniss
Keyword(s):  
Protein Synthesis ◽  
Olive Oil ◽  
Cold Shock ◽  
Polyacrylamide Gel Electrophoresis ◽  
Carbon Sources ◽  
Stress Protein ◽  
Tween 80 ◽  
Synthesis Temperature ◽  
Cold Shock Protein ◽  
In Cells

The induction of proteins after a 25 to 5°C cold shock in the psychrotrophic Acinetobacter HH1-1 was examined using two-dimensional polyacrylamide gel electrophoresis. In addition, effects of various carbon sources (acetate, Tween 80, and olive oil) on protein synthesis after cold shock were assessed. HH1-1 responded to cold shock by synthesizing both cold shock proteins (csps) and cold acclimation proteins (caps). The synthesis of two csps (89 and 18) was increased 2 h after cold shock by the cells, regardless of the carbon source provided. An additional csp (csp 12), with an estimated molecular mass of 12 kDa, was observed in cells grown in olive oil only. Csp 12 was also synthesized when cells were incubated at 30°C, suggesting that this protein may serve as a general stress protein. In addition to csps, caps were observed post cold shock at 72 h in acetate-grown cells and at 140 h in cells grown in Tween 80 and olive oil. Induction of cold-acclimated periplasmic proteins was observed for cells grown in olive oil only, suggesting cells grown in olive oil may be stressed by low temperatures to a greater extent than cells grown in either acetate or Tween 80.Key words: Acinetobacter, carbon sources, cold shock, protein synthesis, temperature.

Specific effect of oestrone sulphate on protein synthesis and secretion by cultured epithelial cells from guinea-pig endometrium

1989 ◽  
Vol 123 (2) ◽  
pp. 233-NP ◽  
Author(s):  
G. Chaminadas ◽  
M. Alkhalaf ◽  
J. P. Rémy-Martin ◽  
A. Y. Propper ◽  
G. L. Adessi
Keyword(s):  
Protein Synthesis ◽  
Epithelial Cells ◽  
Progesterone Receptor ◽  
Guinea Pig ◽  
Cultured Cells ◽  
Polyacrylamide Gel Electrophoresis ◽  
Specific Effect ◽  
Cellular Proteins ◽  
Oestrone Sulphate ◽  
In Cells

ABSTRACT Patterns of induced protein synthesis and secretion in guinea-pig endometrial epithelial cell cultures in response to oestrone sulphate alone and oestrone sulphate plus progesterone were investigated. Epithelial cells were cultured for 3 days in growth medium, then washed three times in a steroid-free medium. For each experiment, anticytokeratin immunostaining was used to discriminate the epithelial cells from the stromal cells. Only experiments in which the control dishes displayed more than 80% of anticytokeratinimmunostained cells were further processed. After this period oestradiol-17β (20 nmol/l; control), oestradiol-17β (20 nmol/l) plus progesterone (0·5 μmol/l), oestrone sulphate (1 μmol/l) or oestrone sulphate (1 μmol/l) plus progesterone (0·5 μmol/l) were added to the medium for 48 h. An immunocytochemical progesterone receptor assay showed that oestradiol-17β increased the progesterone receptor content of cells, and progesterone added to cultured cells in the presence of oestradiol-17β induced a significant increase in oestrogen sulphotransferase activity assessing the hormone responsiveness of the cultured cells. In these culture conditions and after 16 h of incubation, oestradiol-17β induced a 1·7-fold increase in [3H]thymidine incorporation into DNA, and [35S]methionine incorporation into cellular proteins was linearly increased up to 8 h. Biochemical changes induced by the different hormone treatments were studied by labelling the proteins with a 6-h pulse of [35S]methionine. The proteins present in the medium and in cells were analysed by two-dimensional polyacrylamide gel electrophoresis, followed by fluorography. Addition of oestrone sulphate alone or with progesterone produced a change in the patterns of cellular and secreted proteins compared with those in cells cultured with either oestradiol-17β or oestradiol-17β plus progesterone. Three cellular proteins (Mr < 14 000, isoelectric point (pI) 5·2 and 5·3; Mr 75 000, pI 4·9) and one secreted protein (Mr 155 000, pI 5·6–5·9) were specifically induced and could serve as markers of oestrone sulphate action. Journal of Endocrinology (1989) 123, 233–241

scholarly journals Comparative Genome-Wide Transcriptome Analysis of Brucella suis and Brucella microti Under Acid Stress at pH 4.5: Cold Shock Protein CspA and Dps Are Associated With Acid Resistance of B. microti

2021 ◽  
Vol 12 ◽  
Author(s):  
Jorge A. de la Garza-García ◽  
Safia Ouahrani-Bettache ◽  
Sébastien Lyonnais ◽  
Erika Ornelas-Eusebio ◽  
Luca Freddi ◽  
...  
Keyword(s):  
Transcriptome Analysis ◽  
Protein Misfolding ◽  
Cold Shock ◽  
Stress Protein ◽  
Acid Stress ◽  
Acid Resistance ◽  
Cold Shock Protein ◽  
Physiological Adaptation ◽  
Energy Conditions ◽  
Brucella Suis

Brucellae are facultative intracellular coccobacilli causing brucellosis, one of the most widespread bacterial zoonosis affecting wildlife animals, livestock and humans. The genus Brucella comprises classical and atypical species, such as Brucella suis and Brucella microti, respectively. The latter is characterized by increased metabolic activity, fast growth rates, and extreme acid resistance at pH 2.5, suggesting an advantage for environmental survival. In addition, B. microti is more acid-tolerant than B. suis at the intermediate pH of 4.5. This acid-resistant phenotype of B. microti may have major implications for fitness in soil, food products and macrophages. Our study focused on the identification and characterization of acid resistance determinants of B. suis and B. microti in Gerhardt’s minimal medium at pH 4.5 and 7.0 for 20 min and 2 h by comparative RNA-Seq-based transcriptome analysis, validated by RT-qPCR. Results yielded a common core response in both species with a total of 150 differentially expressed genes, and acidic pH-dependent genes regulated specifically in each species. The identified core response mechanisms comprise proton neutralization or extrusion from the cytosol, participating in maintaining physiological intracellular pH values. Differential expression of 441 genes revealed species-specific mechanisms in B. microti with rapid physiological adaptation to acid stress, anticipating potential damage to cellular components and critical energy conditions. Acid stress-induced genes encoding cold shock protein CspA, pseudogene in B. suis, and stress protein Dps were associated with survival of B. microti at pH 4.5. B. suis response with 284 specifically regulated genes suggested increased acid stress-mediated protein misfolding or damaging, triggering the set-up of repair strategies countering the consequences rather than the origin of acid stress and leading to subsequent loss of viability. In conclusion, our work supports the hypothesis that increased acid stress resistance of B. microti is based on selective pressure for the maintenance of functionality of critical genes, and on specific differential gene expression, resulting in rapid adaptation.

scholarly journals Studies on S-adenosylmethionine–magnesium protoporphyrin methyltransferase in Euglena gracilis strain Z

1969 ◽  
Vol 111 (4) ◽  
pp. 573-582 ◽  
Author(s):  
Jean G. Ebbon ◽  
G. H. Tait
Keyword(s):  
Protein Synthesis ◽  
Euglena Gracilis ◽  
Tween 80 ◽  
Cytoplasmic Protein ◽  
Cytoplasmic Ribosomes ◽  
Chloroplast Fraction ◽  
In Cells

1. An enzyme that methylates magnesium protoporphyrin was detected in extracts of light-grown and dark-grown cells of Euglena gracilis. The activity in light-grown cells is two to three times that in cells grown in the dark. 2. The activity is mainly located in the chloroplast fraction from light-grown cells and in proplastids in dark-grown cells. However, in cells grown either in the light or dark, about 15–20% is found in particle-free supernatant. 3. The chloroplast methylating enzyme was solubilized by the action of Tween 80 and partially purified. The properties were investigated. 4. From experiments in which etiolated cells were illuminated in the presence of inhibitors of chloroplast or cytoplasmic protein synthesis, it appears that the methylating enzyme is made on cytoplasmic ribosomes.

A comparison of the chilling-stress response in two differentially tolerant cultivars of tomato (Lycopersicon esculentum)

1992 ◽  
Vol 70 (3-4) ◽  
pp. 191-198 ◽  
Author(s):  
Randal W. Giroux ◽  
W. Gary Filion
Keyword(s):  
Cold Shock ◽  
Chilling Stress ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein S ◽  
Cold Shock Protein ◽  
Relative Mass ◽  
Temperature Decrease ◽  
Cold Shock Response

The chilling responses of two differentially cold tolerant cultivars of tomato were monitored through in vivo labelling of polypeptides with [35S]methionine, both during a gradual temperature decrease (2 °C/day) and also during a rapid cold shock (4 °C). The polypeptides were separated by one-dimensional sodium dodecyl sulfate – polyacrylamide gel electrophoresis and revealed by fluorography. Both cultivars showed changes in the polypeptide profiles resulting from either chilling treatment. During the gradual temperature decrease, there were few differences exhibited between the two cultivars. However, during cold shock both cultivars showed the altered synthesis of several unique polypeptides. Both cultivars showed the appearance of a 35-kDa polypeptide during the gradual temperature decrease and also during the cold shock. The appearance of three high relative mass polypeptides was found in both cultivars only during the gradual temperature decrease. Treatments with cycloheximide and chloramphenicol suggested that cold-shock polypeptides are both nuclear and organelle encoded. The cold-shock response in roots was different from the response in leaves and between cultivars. A comparison of the two cultivars showed a number of differences in polypeptide synthesis which may be related to increased cold tolerance.Key words: cold-shock protein(s), tomato, chilling stress, acclimation, cold tolerance.

scholarly journals Heat and cold shock protein synthesis in arctic and temperate strains of rhizobia.

1992 ◽  
Vol 58 (9) ◽  
pp. 2846-2853 ◽  
Author(s):  
J Cloutier ◽  
D Prévost ◽  
P Nadeau ◽  
H Antoun
Keyword(s):  
Protein Synthesis ◽  
Cold Shock ◽  
Cold Shock Protein

Study on the transgenic tobacco expressing truncated wheat cold shock protein gene TA3-13 and analysis of disease resistance

2011 ◽  
Vol 33 (5) ◽  
pp. 520-526 ◽  
Author(s):  
Na LI ◽  
Xiu-Zhen DU ◽  
Xiao-Mei PAN ◽  
Jin-Sheng WANG ◽  
Cong-Feng SONG
Keyword(s):  
Disease Resistance ◽  
Transgenic Tobacco ◽  
Cold Shock ◽  
Protein Gene ◽  
Cold Shock Protein

Effect of medium of lowered NaCl concentration on virus release and protein synthesis in cells infected with reticuloendotheliosis virus.

1976 ◽  
Vol 17 (2) ◽  
pp. 446-452 ◽  
Author(s):  
J M Bishop ◽  
R L Maldonado ◽  
R F Garry ◽  
P T Allen ◽  
H R Bose ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Virus Release ◽  
Reticuloendotheliosis Virus ◽  
Nacl Concentration ◽  
In Cells

scholarly journals Burkholderia thailandensis E264 as a promising safe rhamnolipids’ producer towards a sustainable valorization of grape marcs and olive mill pomace

2021 ◽  
Author(s):  
Alif Chebbi ◽  
Massimiliano Tazzari ◽  
Cristiana Rizzi ◽  
Franco Hernan Gomez Tovar ◽  
Sara Villa ◽  
...  
Keyword(s):  
Energy Source ◽  
Olive Oil ◽  
Low Cost ◽  
Carbon Sources ◽  
Burkholderia Thailandensis ◽  
Rhamnolipid Production ◽  
Key Points ◽  
Wide Range ◽  
Long Chain ◽  
Olive Mill

Abstract Within the circular economy framework, our study aims to assess the rhamnolipid production from winery and olive oil residues as low-cost carbon sources by nonpathogenic strains. After evaluating various agricultural residues from those two sectors, Burkholderia thailandensis E264 was found to use the raw soluble fraction of nonfermented (white) grape marcs (NF), as the sole carbon and energy source, and simultaneously, reducing the surface tension to around 35 mN/m. Interestingly, this strain showed a rhamnolipid production up to 1070 mg/L (13.37 mg/g of NF), with a higher purity, on those grape marcs, predominately Rha-Rha C14-C14, in MSM medium. On olive oil residues, the rhamnolipid yield of using olive mill pomace (OMP) at 2% (w/v) was around 300 mg/L (15 mg/g of OMP) with a similar CMC of 500 mg/L. To the best of our knowledge, our study indicated for the first time that a nonpathogenic bacterium is able to produce long-chain rhamnolipids in MSM medium supplemented with winery residues, as sole carbon and energy source. Key points • Winery and olive oil residues are used for producing long-chain rhamnolipids (RLs). • Both higher RL yields and purity were obtained on nonfermented grape marcs as substrates. • Long-chain RLs revealed stabilities over a wide range of pH, temperatures, and salinities

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