scholarly journals Structural analysis of .BETA.-glucans from a killer toxin sensitive yeast, Saccharomyces cerevisiae, and a killer-resistant mutant.

1989 ◽  
Vol 53 (7) ◽  
pp. 1983-1985 ◽  
Author(s):  
Tasuku NAKAJIMA ◽  
Keishi AOYAMA ◽  
Eiji ICHISHIMA ◽  
Kazuo MATSUDA
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Structural Analysis ◽  
Killer Toxin ◽  
Resistant Mutant ◽  
Yeast Saccharomyces Cerevisiae ◽  
Beta Glucans

8-Azaguanine Resistant Mutant of the Yeast,Saccharomyces cerevisiae

1986 ◽  
Vol 50 (5) ◽  
pp. 1339-1340
Author(s):  
Naoko Sato ◽  
Makoto Shimosaka ◽  
Yasuki Fukuda ◽  
Kousaku Murata ◽  
Akira Kimura
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Resistant Mutant ◽  
Yeast Saccharomyces Cerevisiae

scholarly journals A heat shock-resistant mutant of Saccharomyces cerevisiae shows constitutive synthesis of two heat shock proteins and altered growth.

1984 ◽  
Vol 99 (4) ◽  
pp. 1441-1450 ◽  
Author(s):  
H Iida ◽  
I Yahara
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Heat Shock ◽  
Type Strain ◽  
Wild Type Strain ◽  
Growth Control ◽  
Protein S ◽  
Resistant Mutant ◽  
Wild Type ◽  
Yeast Saccharomyces Cerevisiae ◽  
Sulfur Starvation

A heat shock-resistant mutant of the budding yeast Saccharomyces cerevisiae was isolated at the mutation frequency of 10(-7) from a culture treated with ethyl methane sulfonate. Cells of the mutant are approximately 1,000-fold more resistant to lethal heat shock than those of the parental strain. Tetrad analysis indicates that phenotypes revealed by this mutant segregated together in the ratio 2+:2- from heterozygotes constructed with the wild-type strain of the opposite mating type, and are, therefore, attributed to a single nuclear mutation. The mutated gene in the mutant was herein designated hsr1 (heat shock response). The hsr1 allele is recessive to the HSR1+ allele of the wild-type strain. Exponentially growing cells of hsr1 mutant were found to constitutively synthesize six proteins that are not synthesized or are synthesized at reduced rates in HSR1+ cells unless appropriately induced. These proteins include one hsp/G0-protein (hsp48A), one hsp (hsp48B), and two G0-proteins (p73, p56). Heterozygous diploid (hsr1/HSR1+) cells do not synthesize the proteins constitutively induced in hsr1 cells, which suggests that the product of the HSR1 gene might negatively regulate the synthesis of these proteins. The hsr1 mutation also led to altered growth of the mutant cells. The mutation elongated the duration of G1 period in the cell cycle and affected both growth arrest by sulfur starvation and growth recovery from it. We discuss the problem of which protein(s) among those constitutively expressed in growing cells of the hsr1 mutant is responsible for heat shock resistance and alterations in the growth control.

scholarly journals Immunolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae.

1991 ◽  
Vol 113 (3) ◽  
pp. 527-538 ◽  
Author(s):  
K Redding ◽  
C Holcomb ◽  
R S Fuller
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Secretory Pathway ◽  
Killer Toxin ◽  
Proteolytic Processing ◽  
Yeast Cells ◽  
Yeast Saccharomyces Cerevisiae ◽  
Golgi Compartment ◽  
Membrane Bound ◽  
Gene Structures ◽  
Stage Analysis

The Kex2 protein of the yeast Saccharomyces cerevisiae is a membrane-bound, Ca2(+)-dependent serine protease that cleaves the precursors of the mating pheromone alpha-factor and the M1 killer toxin at pairs of basic residues during their transport through the secretory pathway. To begin to characterize the intracellular locus of Kex2-dependent proteolytic processing, we have examined the subcellular distribution of Kex2 protein in yeast by indirect immunofluorescence. Kex2 protein is located at multiple, discrete sites within wild-type yeast cells (average, 3.0 +/- 1.7/mother cell). Qualitatively similar fluorescence patterns are observed at elevated levels of expression, but no signal is found in cells lacking the KEX2 gene. Structures containing Kex2 protein are not concentrated at a perinuclear location, but are distributed throughout the cytoplasm at all phases of the cell cycle. Kex2-containing structures appear in the bud at an early, premitotic stage. Analysis of conditional secretory (sec) mutants demonstrates that Kex2 protein ordinarily progresses from the ER to the Golgi but is not incorporated into secretory vesicles, consistent with the proposed localization of Kex2 protein to the yeast Golgi complex.

scholarly journals Selective system based on fragments of the M1 virus for the yeast Saccharomyces cerevisiae transformation

2020 ◽  
Author(s):  
Dmitri Mikhailovich Muzaev ◽  
Andrey Mikhailovitch Rumyantsev ◽  
Ousama Raek Al Shanaa ◽  
Elena Viktorovna Sambuk
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Homologous Recombination ◽  
Killer Toxin ◽  
Recipient Strain ◽  
Expression Cassette ◽  
Yeast Saccharomyces Cerevisiae ◽  
Selective System ◽  
Dna Fragment ◽  
Sequence Encoding ◽  
Gal1 Gene

Background. A selective system based on the M1 virus of the yeast Saccharomyces cerevisiae was proposed. Methods. To create a recipient strain, a DNA fragment encoding the killer toxin of the M1 virus under the control of the regulated promoter of the GAL1 gene was inserted into the genome of S. cerevisiae strains Y-1236 and Y-2177. Results. Integration of such expression cassette leads to the conditional lethality - resulting strains die on a medium with galactose when killer toxin synthesis occurs. A linear DNA fragment containing the gene of interest flanked by sequences homologous to the promoter of the GAL1 gene and the termination region of the CYC1 gene is used to transform the obtained strains. During transformation due to homologous recombination, the sequence encoding the killer toxin is cleaved and the transformants grow on a medium with galactose. Conclusion. The proposed selective system combines the main advantages of other systems: the use of simple media, without the need to add expensive antibiotics, and a simplified technique for constructing expression cassettes and selecting transformants.

Structural analysis of lipid particles from the yeast Saccharomyces cerevisiae

2007 ◽  
Vol 149 ◽  
pp. S27
Author(s):  
Karlheinz Grillitsch ◽  
Tibor Czabany ◽  
Andrea Wagner ◽  
Dagmar Zweytick ◽  
Elisabeth Ingolic ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Structural Analysis ◽  
Yeast Saccharomyces Cerevisiae ◽  
Lipid Particles

Toxicité génétique du chlorure de méthylmercure (CH3HgCl) sur les mitochondries de Saccharomyces cerevisiae

1983 ◽  
Vol 29 (9) ◽  
pp. 1149-1153 ◽  
Author(s):  
J. Phipps ◽  
D. R. Miller
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Dose Response ◽  
Resistant Mutant ◽  
Dna Lesions ◽  
Organic Form ◽  
Yeast Saccharomyces Cerevisiae ◽  
Mechanism Of Toxicity

Among the strains of the yeast Saccharomyces cerevisiae we investigated, the organic form of mercury:methylmercury (II) does not seem to induce any cytoplasmic mutant "petite colonie" rho−. However, it induces a significant number of the erythromycin-resistant mutant Eryr. A dose response is shown. These effects are discussed in the view of the part that discrete DNA lesions could take in the explanation of the mechanism of toxicity of the organomercurial.

scholarly journals 8-Azaguanine resistant mutant of the yeast, Saccharomyces cerevisiae.

1986 ◽  
Vol 50 (5) ◽  
pp. 1339-1340 ◽  
Author(s):  
Naoko SATO ◽  
Makoto SHIMOSAKA ◽  
Yasuki FUKUDA ◽  
Kousaku MURATA ◽  
Akira KIMURA
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Resistant Mutant ◽  
Yeast Saccharomyces Cerevisiae

scholarly journals INVESTIGATION OF THE STRUCTURE OF WATER-SOLUBLE GLUCAN YEAST SACCHAROMYCES CEREVISIAE

2020 ◽  
Vol 14 (2) ◽  
Author(s):  
N. Cherno ◽  
K. Naumenko
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Physiological Activity ◽  
Physiological Effect ◽  
Water Soluble ◽  
Beta Glucan ◽  
Yeast Saccharomyces Cerevisiae ◽  
Solubility In Water ◽  
Beta Glucans ◽  
Maximum Water

It is known that a well-functioning immune system is important for human health. There are many natural and synthetic preparation that are widely used as immunomodulators. One such natural preparat is β-glucan. Beta-glucans are a group of natural polysaccharides. They are recognized as an effective immunocorrector. Their use is advisable both for the prevention of immunodeficiency pathologies and for the complex treatment of many diseases from cardiovascular to oncological. The physiological activity of β-glucan depends on the type and configuration between monosaccharide residues, branching and conformation of macromolecules, solubility in water. One major source of β-glucan is the baker’s yeast Saccharomyces cerevisiae. Much research has been carried out over the years examining cell wall glucans from Saccharomyces cerevisiae. This work is the development devoted to the characterization of water-soluble beta-glucan obtained as a result of controlled degradation with the enzyme Rovabio Excel AP of glucan cell walls of yeast Saccharomyces cerevisiae. In this study conditions were selected which allow to accumulate the maximum water-soluble fractions with a molecular mass of 1–30 kDa presumably as fractions with a high immunomodulatory effect. The results of the paper show that glucan can be isolated from Saccharomyces cerevisiae in very pure form by the method used in this study. Thus structural analysis gives reliable results. The structural characterization of pure product was performed using the common analytical procedures: enzymes hudrolyses and spectral analyses FTIR, NMR spectroscopy. On the basis of the obtained results it was concluded that  investigated glucan is a (1→3)-β-linked glucose polymer with (1→6)-β-linked side chains with sparsely branched. Further work will concern the physiological effect of water-soluble glucan in comparision to the native glucan. The structural requirements for example for an immunomodulation in humans or animals are still under discussion.

scholarly journals A Rapid Method for Sequencing Double-Stranded RNAs Purified from Yeasts and the Identification of a Potent K1 Killer Toxin Isolated from Saccharomyces cerevisiae

Viruses ◽  
2019 ◽  
Vol 11 (1) ◽  
pp. 70 ◽  
Author(s):  
Angela Crabtree ◽  
Emily Kizer ◽  
Samuel Hunter ◽  
James Van Leuven ◽  
Daniel New ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Next Generation Sequencing ◽  
Killer Toxin ◽  
Next Generation ◽  
High Quality ◽  
Yeast Saccharomyces Cerevisiae ◽  
Single Strain ◽  
Double Stranded Rna ◽  
Generation Sequencing ◽  
K1 Toxin

Mycoviruses infect a large number of diverse fungal species, but considering their prevalence, relatively few high-quality genome sequences have been determined. Many mycoviruses have linear double-stranded RNA genomes, which makes it technically challenging to ascertain their nucleotide sequence using conventional sequencing methods. Different specialist methodologies have been developed for the extraction of double-stranded RNAs from fungi and the subsequent synthesis of cDNAs for cloning and sequencing. However, these methods are often labor-intensive, time-consuming, and can require several days to produce cDNAs from double-stranded RNAs. Here, we describe a comprehensive method for the rapid extraction and sequencing of dsRNAs derived from yeasts, using short-read next generation sequencing. This method optimizes the extraction of high-quality double-stranded RNAs from yeasts and 3′ polyadenylation for the initiation of cDNA synthesis for next-generation sequencing. We have used this method to determine the sequence of two mycoviruses and a double-stranded RNA satellite present within a single strain of the model yeast Saccharomyces cerevisiae. The quality and depth of coverage was sufficient to detect fixed and polymorphic mutations within viral populations extracted from a clonal yeast population. This method was also able to identify two fixed mutations within the alpha-domain of a variant K1 killer toxin encoded on a satellite double-stranded RNA. Relative to the canonical K1 toxin, these newly reported mutations increased the cytotoxicity of the K1 toxin against a specific species of yeast.

Sign in / Sign up

Export Citation Format

Share Document