A Biosensor for Express Assessment of Integral Toxicity of Polymer- and Textile-Based Products

2021 ◽  
Vol 37 (6) ◽  
pp. 119-128
Author(s):  
M.G. Zaitsev ◽  
V.A. Arlyapov ◽  
V.A. Alferov ◽  
O.N. Ponamoreva ◽  
A.N. Reshetilov
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Lemna Minor ◽  
Oxygen Electrode ◽  
Standard Test ◽  
Yeast Saccharomyces Cerevisiae ◽  
Immobilized Bacteria ◽  
Toxic Pollutants ◽  
The Russian Federation ◽  
Stylonychia Mytilus

Biosensors to assess integral toxicity, which consist of an oxygen electrode and immobilized bacteria (Gluconobacter оxydans B-1280 and Escherichia coli К802) or yeast (Saccharomyces cerevisiae Y-1173) have been designed. Model toxic pollutants (phenol, n-nitrophenol, formaldehyde and heavy metal ions Pb2+, Cu2+, Hg2+ and Cr2O72) were chosen to estimate the concentration, at which 50% inhibition of glucose oxidation (ЕC50) was observed. It was shown that a biosensor based on G. оxydans cells provides the most sensitive detection of toxic pollutants, exhibits long operational stability (36 days) and can be used for the detection of integral toxicity. It was shown that the assessment of the toxicity of industrially manufactured polymer- and textile-based products using the developed biosensors and standard test systems (duckweed Lemna minor and protozoa ciliates Stylonychia mytilus) gave similar results. The proposed biosensors can significantly reduce the analysis time compared to the normatively fixed biotesting methods and can be used as a prototype of serial integral toxicity analyzers. biosensor, toxicity, immobilized bacteria Gluconobacter оxydans, Escherichia coli and yeast Saccharomyces cerevisiae, biotesting This research was supported by the State Task of the Ministry of Science and Higher Education of the Russian Federation (no. FEWG-2020-0008).

scholarly journals Composition of the λ plasmid heritable replicationcomplex

2002 ◽  
Vol 364 (3) ◽  
pp. 857-862 ◽  
Author(s):  
Katarzyna POTRYKUS ◽  
Sylwia BARAŃSKA ◽  
Alicja WĘGRZYN ◽  
Grzegorz WĘGRZYN
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Protein Synthesis ◽  
Plasmid Dna ◽  
Pcr Analysis ◽  
Cross Linking ◽  
Bacteriophage Λ ◽  
Yeast Saccharomyces Cerevisiae ◽  
Replication Complex

Previous studies indicated during replication of plasmids derived from bacteriophage λ (the so-called λ plasmids), that, once assembled, replication complex can be inherited by one of the two daughter plasmid copies after each replication round, and may function in subsequent replication rounds. It seems that similar processes occur during replication of other DNA molecules, including chromosomes of the yeast Saccharomyces cerevisiae. However, apart from some suggestions based on genetic experiments, composition of the λ heritable replication complex remains unknown. In amino acid-starved Escherichia coli relA mutants, replication of λ plasmid DNA is carried out exclusively by the heritable replication complex as assembly of new complexes is impaired due to inhibition of protein synthesis. Here, using a procedure based on in vivo cross-linking, cell lysis, immunoprecipitation with specific sera, de-cross-linking and PCR analysis, we demonstrate that the λ heritable replication complex consists of O, P, DnaB and, perhaps surprisingly, DnaK proteins.

scholarly journals Saccharomyces cerevisiae displays an increased growth rate and an extended replicative lifespan when grown under respiratory conditions in the presence of bacteria

2017 ◽  
Vol 63 (9) ◽  
pp. 806-810
Author(s):  
Paul A. Kirchman ◽  
Nicholas Van Zee
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Growth Rate ◽  
Volatile Compound ◽  
Lifespan Extension ◽  
Yeast Saccharomyces Cerevisiae ◽  
Replicative Lifespan ◽  
Solid Media ◽  
Respiratory Conditions ◽  
Ferment Glucose

Individual cells of the budding yeast Saccharomyces cerevisiae have a limited replicative potential, referred to as the replicative lifespan. We have found that both the growth rate and average replicative lifespan of S. cerevisiae cells are greatly increased in the presence of a variety of bacteria. The growth and lifespan effects are not observable when yeast are allowed to ferment glucose but are only notable on solid media when yeast are forced to respire due to the lack of a fermentable carbon source. Growth near strains of Escherichia coli containing deletions of genes needed for the production of compounds used for quorum sensing or for the production of the siderophore enterobactin also still induced the lifespan extension in yeast. Furthermore, the bacterially induced increases in growth rate and lifespan occur even across gaps in the growth medium, indicating that the bacteria are influencing the yeast through the action of a volatile compound.

scholarly journals Research of the inactivation of pathogens in water under exposure to low temperature plasma

2019 ◽  
Vol 95 (6) ◽  
pp. 588-592 ◽  
Author(s):  
V. A. Kolesnikov ◽  
Roman Yakushin ◽  
V. A. Brodsky ◽  
E. S. Babusenko ◽  
A. V. Chistolinov
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Bacillus Subtilis ◽  
Low Temperature ◽  
Detrimental Effect ◽  
Coliform Bacteria ◽  
Low Temperature Plasma ◽  
Yeast Saccharomyces Cerevisiae ◽  
Temperature Plasma ◽  
General Decline

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.

Heat shock-regulated production of Escherichia coli beta-galactosidase in Saccharomyces cerevisiae

1983 ◽  
Vol 3 (9) ◽  
pp. 1625-1633
Author(s):  
D B Finkelstein ◽  
S Strausberg
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Heat Shock ◽  
Plasmid Vector ◽  
Lacz Gene ◽  
Multicopy Plasmid ◽  
Yeast Saccharomyces Cerevisiae ◽  
Reading Frame ◽  
Inducible Synthesis ◽  
Beta Galactosidase

The HSP90 gene of the yeast Saccharomyces cerevisiae encodes a heat shock-inducible protein with an Mr of 90,000 (hsp90) and unknown function. We fused DNA fragments of a known sequence (namely, either end of a 1.4-kilobase EcoRI fragment which contains the S. cerevisiae TRP1 gene) to an EcoRI site within the coding sequence of the HSP90 gene. When these fusions are introduced into S. cerevisiae they direct the synthesis of unique truncated hsp90 proteins. By determining the size and charge of these proteins we were able to deduce the translational reading frame at the (EcoRI) fusion site. This information allowed us to design and construct a well-defined in-frame fusion between the S. cerevisiae HSP90 gene and the Escherichia coli lacZ gene. When this fused gene is introduced into S. cerevisiae on a multicopy plasmid vector, it directs the heat shock-inducible synthesis of a fused protein, which is an enzymatically active beta-galactosidase. Thus, for the first time, it is possible to quantitate the heat shock response in a eucaryotic organism with a simple enzyme assay.

Cloned �-galactosidase gene of Escherichia coli is expressed in the yeast Saccharomyces cerevisiae

1980 ◽  
Vol 2 (2) ◽  
pp. 109-113 ◽  
Author(s):  
Jean-Jacques Panthier ◽  
Philippe Fournier ◽  
Henri Heslot ◽  
Alain Rambach
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Yeast Saccharomyces Cerevisiae

ETHANOL AS A MODIFIER OF RADIATION SENSITIVITY OF LIVING CELLS AGAINST UV-C RADIATION

2019 ◽  
Vol 186 (2-3) ◽  
pp. 191-195
Author(s):  
Barbora Neužilová ◽  
Lukáš Ondrák ◽  
Václav Čuba ◽  
Viliam Múčka
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Dose Rate ◽  
Ethanol Concentration ◽  
Radiation Sensitivity ◽  
Living Cells ◽  
Yeast Saccharomyces Cerevisiae ◽  
Escherichia Coli Bacteria ◽  
Uv C

ABSTRACT The protection of Escherichia coli bacteria and the yeast Saccharomyces cerevisiae against UV-C radiation by ethanol was studied. It was found that the fraction of surviving cells increases with increasing ethanol concentration. The specific protection depends on the dose rate, concentration range of ethanol, and it is higher for yeast compared to the bacteria.

The Escherichia coli recA gene increases resistance of the yeast Saccharomyces cerevisiae to ionizing and ultraviolet radiation

1991 ◽  
Vol 227 (3) ◽  
pp. 473-480 ◽  
Author(s):  
Jela Brozmanová ◽  
Ľubica Černáková ◽  
Viera Vlčková ◽  
Jozef Duraj ◽  
Ivana Fridrichová
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Ultraviolet Radiation ◽  
Reca Gene ◽  
Yeast Saccharomyces Cerevisiae

Expression of the Escherichia coli recA gene in the yeast Saccharomyces cerevisiae

Biochimie ◽  
1991 ◽  
Vol 73 (2-3) ◽  
pp. 285-288 ◽  
Author(s):  
L. Cernakova ◽  
I. Fridrichova ◽  
M. Pirsel ◽  
K. Kleibl ◽  
J. Duraj ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Reca Gene ◽  
Yeast Saccharomyces Cerevisiae

scholarly journals Heat shock-regulated production of Escherichia coli beta-galactosidase in Saccharomyces cerevisiae.

1983 ◽  
Vol 3 (9) ◽  
pp. 1625-1633 ◽  
Author(s):  
D B Finkelstein ◽  
S Strausberg
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Heat Shock ◽  
Plasmid Vector ◽  
Lacz Gene ◽  
Multicopy Plasmid ◽  
Yeast Saccharomyces Cerevisiae ◽  
Reading Frame ◽  
Inducible Synthesis ◽  
Beta Galactosidase

The HSP90 gene of the yeast Saccharomyces cerevisiae encodes a heat shock-inducible protein with an Mr of 90,000 (hsp90) and unknown function. We fused DNA fragments of a known sequence (namely, either end of a 1.4-kilobase EcoRI fragment which contains the S. cerevisiae TRP1 gene) to an EcoRI site within the coding sequence of the HSP90 gene. When these fusions are introduced into S. cerevisiae they direct the synthesis of unique truncated hsp90 proteins. By determining the size and charge of these proteins we were able to deduce the translational reading frame at the (EcoRI) fusion site. This information allowed us to design and construct a well-defined in-frame fusion between the S. cerevisiae HSP90 gene and the Escherichia coli lacZ gene. When this fused gene is introduced into S. cerevisiae on a multicopy plasmid vector, it directs the heat shock-inducible synthesis of a fused protein, which is an enzymatically active beta-galactosidase. Thus, for the first time, it is possible to quantitate the heat shock response in a eucaryotic organism with a simple enzyme assay.

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