Significance of the lag phase in K1 killer toxin action on sensitive yeast cells

1995 ◽  
Vol 40 (2) ◽  
pp. 213-215 ◽  
Author(s):  
H. Kurzweilová ◽  
K. Sigler
Keyword(s):  
Killer Toxin ◽  
Yeast Cells ◽  
Lag Phase

The effects of starvation and acidification on lag phase duration of surviving yeast cells

2018 ◽  
Vol 275 ◽  
pp. 60-64 ◽  
Author(s):  
Kenichi Shibata ◽  
Kohei Obase ◽  
Kiminori Itoh ◽  
Takashi Amemiya
Keyword(s):  
Yeast Cells ◽  
Lag Phase ◽  
Phase Duration

Kluyveromyces lactis killer toxin inhibits adenylate cyclase of sensitive yeast cells

Nature ◽  
1983 ◽  
Vol 304 (5925) ◽  
pp. 464-466 ◽  
Author(s):  
Yuji Sugisaki ◽  
Norio Gunge ◽  
Kenji Sakaguchi ◽  
Makari Yamasaki ◽  
Gakuzo Tamura
Keyword(s):  
Adenylate Cyclase ◽  
Kluyveromyces Lactis ◽  
Killer Toxin ◽  
Yeast Cells

scholarly journals Effects of Low-Shear Modeled Microgravity on Cell Function, Gene Expression, and Phenotype in Saccharomyces cerevisiae

2006 ◽  
Vol 72 (7) ◽  
pp. 4569-4575 ◽  
Author(s):  
B. Purevdorj-Gage ◽  
K. B. Sheehan ◽  
L. E. Hyman
Keyword(s):  
Gene Expression ◽  
Saccharomyces Cerevisiae ◽  
Cell Function ◽  
Yeast Cells ◽  
Lag Phase ◽  
Limited Information ◽  
Cellular Functions ◽  
Modeled Microgravity ◽  
Expression Of Genes ◽  
Low Shear

ABSTRACT Only limited information is available concerning the effects of low-shear modeled microgravity (LSMMG) on cell function and morphology. We examined the behavior of Saccharomyces cerevisiae grown in a high-aspect-ratio vessel, which simulates the low-shear and microgravity conditions encountered in spaceflight. With the exception of a shortened lag phase (90 min less than controls; P < 0.05), yeast cells grown under LSMMG conditions did not differ in growth rate, size, shape, or viability from the controls but did differ in the establishment of polarity as exhibited by aberrant (random) budding compared to the usual bipolar pattern of controls. The aberrant budding was accompanied by an increased tendency of cells to clump, as indicated by aggregates containing five or more cells. We also found significant changes (greater than or equal to twofold) in the expression of genes associated with the establishment of polarity (BUD5), bipolar budding (RAX1, RAX2, and BUD25), and cell separation (DSE1, DSE2, and EGT2). Thus, low-shear environments may significantly alter yeast gene expression and phenotype as well as evolutionary conserved cellular functions such as polarization. The results provide a paradigm for understanding polarity-dependent cell responses to microgravity ranging from pathogenesis in fungi to the immune response in mammals.

scholarly journals A new protocol for single-cell RNA-seq reveals stochastic gene expression during lag phase in budding yeast

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Abbas Jariani ◽  
Lieselotte Vermeersch ◽  
Bram Cerulus ◽  
Gemma Perez-Samper ◽  
Karin Voordeckers ◽  
...  
Keyword(s):  
Single Cell ◽  
Rna Sequencing ◽  
Mammalian Cells ◽  
Yeast Cells ◽  
Lag Phase ◽  
Rna Seq ◽  
Molecular Processes ◽  
Sequencing Technology ◽  
Single Cell Rna Sequencing ◽  
Order Of Magnitude

Current methods for single-cell RNA sequencing (scRNA-seq) of yeast cells do not match the throughput and relative simplicity of the state-of-the-art techniques that are available for mammalian cells. In this study, we report how 10x Genomics’ droplet-based single-cell RNA sequencing technology can be modified to allow analysis of yeast cells. The protocol, which is based on in-droplet spheroplasting of the cells, yields an order-of-magnitude higher throughput in comparison to existing methods. After extensive validation of the method, we demonstrate its use by studying the dynamics of the response of isogenic yeast populations to a shift in carbon source, revealing the heterogeneity and underlying molecular processes during this shift. The method we describe opens new avenues for studies focusing on yeast cells, as well as other cells with a degradable cell wall.

Killer Toxins of Yeasts: Inhibitors of Fermentation and Their Adsorption

1987 ◽  
Vol 50 (3) ◽  
pp. 234-238 ◽  
Author(s):  
FERDINAND RADLER ◽  
MANFRED SCHMITT
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Yeast Cell ◽  
Cell Walls ◽  
Killer Toxin ◽  
Yeast Cells ◽  
Toxin Concentration ◽  
Commercial Preparation ◽  
Killer Toxins ◽  
Original Amount

The killer toxin (KT 28), a glycoprotein of Saccharomyces cerevisiae strain 28, was almost completely adsorbed by bentonite, when applied at a concentration of 1 g per liter. No significant differences were found between several types of bentonite. Killer toxin KT 28 is similarly adsorbed by intact yeast cells or by a commercial preparation of yeast cell walls that has been recommended to prevent stuck fermentations. An investigation of the cell wall fractions revealed that the toxin KT 28 was mainly adsorbed by mannan, that removed the toxin completely. The alkali-soluble and the alkali-insoluble β-1,3- and β-1,6-D-glucans lowered the toxin concentration to one tenth of the original amount. The killer toxin of the type K1 of S. cerevisiae was adsorbed much better by glucans than by mannan.

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.

Kinetic studies of killer toxin K1 binding to yeast cells indicate two receptor populations

1994 ◽  
Vol 162 (3) ◽  
pp. 211-214 ◽  
Author(s):  
Helena Kurzweilov� ◽  
Karel Sigler
Keyword(s):  
Killer Toxin ◽  
Kinetic Studies ◽  
Yeast Cells

Changes of trehalose content and expression of relative genes during the bioethanol fermentation bySaccharomyces cerevisiae

2016 ◽  
Vol 62 (10) ◽  
pp. 827-835 ◽  
Author(s):  
Chenfeng Yi ◽  
Fenglian Wang ◽  
Shijun Dong ◽  
Hao Li
Keyword(s):  
Phase Transition ◽  
Stationary Phase ◽  
Ethanol Tolerance ◽  
Stationary Phases ◽  
Exponential Phase ◽  
Yeast Cells ◽  
Ethanol Stress ◽  
Lag Phase ◽  
Significant Difference ◽  
Trehalose Content

Traditionally, trehalose is considered as a protectant to improve the ethanol tolerance of Saccharomyces cerevisiae. In this study, to clarify the changes and roles of trehalose during the bioethanol fermentation, trehalose content and expression of related genes at lag, exponential, and stationary phases (i.e., 2, 8, and 16 h of batch fermentation process) were determined. Although yeast cells at exponential and stationary phase had higher trehalose content than cells at lag phase (P < 0.01), there was no significant difference in trehalose content between exponential and stationary phases (P > 0.05). Moreover, expression of the trehalose degradation-related genes NTH1 and NTH2 decreased at exponential phase in comparison with that at lag phase; compared with cells at lag phase, cells at stationary phase had higher expression of TPS1, ATH1, NTH1, and NTH2 but lower expression of TPS2. During the lag–exponential phase transition, downregulation of NTH1 and NTH2 promoted accumulation of trehalose, and to some extent, trehalose might confer ethanol tolerance to S. cerevisiae before stationary phase. During the exponential–stationary phase transition, upregulation of TPS1 contributed to accumulation of trehalose, and Tps1 protein might be indispensable in yeast cells to withstand ethanol stress at the stationary phase. Moreover, trehalose would be degraded to supply carbon source at stationary phase.

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