scholarly journals Metabolism of 3-deoxy-3-fluoro-d-mannose and 4-deoxy-4-fluoro-d-mannose by Saccharomyces cerevisiae S288C

1983 ◽  
Vol 209 (3) ◽  
pp. 677-685 ◽  
Author(s):  
T J Grier ◽  
J R Rasmussen
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Particulate Fraction ◽  
Radioactive Material ◽  
Yeast Cells ◽  
Cell Wall Fraction ◽  
Cell Wall Polysaccharides ◽  
Sugar Nucleotide ◽  
Mannose 6 Phosphate

Incubation of Saccharomyces cerevisiae S288C with 4-deoxy-4-fluoro-D-[1-14C]-mannose resulted in the formation of three metabolites that were characterized as 4-deoxy-4-fluoro-D-[1-14C]mannose 1,6-bisphosphate, 4-deoxy-4-fluoro-D-[1-14C]-mannose 6-phosphate and GDP-4-deoxy-4-fluoro-D-[1-14C]mannose. In addition, radioactive material was incorporated into a particulate fraction composed primarily of cell-wall polysaccharides. Compared with the 4-fluoro sugar, 3-deoxy-3-fluoro-D-[1-14C]mannose was not transported into yeast cells as well, and its conversion into sugar nucleotide was much less efficient. Metabolites that were isolated after incubation with the 3-fluoro analogue were identified as 3-deoxy-3-fluoro-D-[1-14C]mannose 1,6-bisphosphate, 3-deoxy-3-fluoro-D-[1-14C]mannose 6-phosphate and GDP-3-deoxy-3-fluoro-D-[1-14C]mannose. Little radioactivity was transferred into the cell-wall fraction.

scholarly journals Purification of profilin from Saccharomyces cerevisiae and analysis of profilin-deficient cells.

1990 ◽  
Vol 110 (1) ◽  
pp. 105-114 ◽  
Author(s):  
B K Haarer ◽  
S H Lillie ◽  
A E Adams ◽  
V Magdolen ◽  
W Bandlow ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Actin Polymerization ◽  
Yeast Cells ◽  
Predicted Amino Acid Sequence ◽  
Temperature Sensitive ◽  
Wild Type ◽  
Yeast Saccharomyces Cerevisiae ◽  
Ellipsoidal Shape ◽  
Hydrolysis Of

We have isolated profilin from yeast (Saccharomyces cerevisiae) and have microsequenced a portion of the protein to confirm its identity; the region microsequenced agrees with the predicted amino acid sequence from a profilin gene recently isolated from S. cerevisiae (Magdolen, V., U. Oechsner, G. Müller, and W. Bandlow. 1988. Mol. Cell. Biol. 8:5108-5115). Yeast profilin resembles profilins from other organisms in molecular mass and in the ability to bind to polyproline, retard the rate of actin polymerization, and inhibit hydrolysis of ATP by monomeric actin. Using strains that carry disruptions or deletions of the profilin gene, we have found that, under appropriate conditions, cells can survive without detectable profilin. Such cells grow slowly, are temperature sensitive, lose the normal ellipsoidal shape of yeast cells, often become multinucleate, and generally grow much larger than wild-type cells. In addition, these cells exhibit delocalized deposition of cell wall chitin and have dramatically altered actin distributions.

scholarly journals The effect of Saccharomyces cerevisiae and Aspergillus oryzae on the digestion of the cell wall fraction of a mixed diet in defaunated and refaunated sheep rumen

1998 ◽  
Vol 38 (4) ◽  
pp. 401-416 ◽  
Author(s):  
Jean-Pierre Jouany ◽  
Frédérique Mathieu ◽  
Jean Senaud ◽  
Jacques Bohatier ◽  
Gérard Bertin ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Aspergillus Oryzae ◽  
Mixed Diet ◽  
Cell Wall Fraction ◽  
Sheep Rumen

scholarly journals Deletion of Atg22 gene contributes to reduce programmed cell death induced by acetic acid stress in Saccharomyces cerevisiae

2019 ◽  
Vol 12 (1) ◽  
Author(s):  
Jingjin Hu ◽  
Yachen Dong ◽  
Wei Wang ◽  
Wei Zhang ◽  
Hanghang Lou ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Cell Death ◽  
Cell Wall ◽  
Acetic Acid ◽  
Programmed Cell Death ◽  
Cell Wall Integrity ◽  
Yeast Cells ◽  
Death Process ◽  
Lignocellulosic Biofuel

Abstract Background Programmed cell death (PCD) induced by acetic acid, the main by-product released during cellulosic hydrolysis, cast a cloud over lignocellulosic biofuel fermented by Saccharomyces cerevisiae and became a burning problem. Atg22p, an ignored integral membrane protein located in vacuole belongs to autophagy-related genes family; prior study recently reported that it is required for autophagic degradation and efflux of amino acids from vacuole to cytoplasm. It may alleviate the intracellular starvation of nutrition caused by Ac and increase cell tolerance. Therefore, we investigate the role of atg22 in cell death process induced by Ac in which attempt is made to discover new perspectives for better understanding of the mechanisms behind tolerance and more robust industrial strain construction. Results In this study, we compared cell growth, physiological changes in the absence and presence of Atg22p under Ac exposure conditions. It is observed that disruption and overexpression of Atg22p delays and enhances acetic acid-induced PCD, respectively. The deletion of Atg22p in S. cerevisiae maintains cell wall integrity, and protects cytomembrane integrity, fluidity and permeability upon Ac stress by changing cytomembrane phospholipids, sterols and fatty acids. More interestingly, atg22 deletion increases intracellular amino acids to aid yeast cells for tackling amino acid starvation and intracellular acidification. Further, atg22 deletion upregulates series of stress response genes expression such as heat shock protein family, cell wall integrity and autophagy. Conclusions The findings show that Atg22p possessed the new function related to cell resistance to Ac. This may help us have a deeper understanding of PCD induced by Ac and provide a new strategy to improve Ac resistance in designing industrial yeast strains for bioethanol production during lignocellulosic biofuel fermentation.

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 Evidence for a Role for the Plasma Membrane in the Nanomechanical Properties of the Cell Wall as Revealed by an Atomic Force Microscopy Study of the Response of Saccharomyces cerevisiae to Ethanol Stress

2016 ◽  
Vol 82 (15) ◽  
pp. 4789-4801 ◽  
Author(s):  
Marion Schiavone ◽  
Cécile Formosa-Dague ◽  
Carolina Elsztein ◽  
Marie-Ange Teste ◽  
Helene Martin-Yken ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Atomic Force Microscopy ◽  
Cell Wall ◽  
Cell Membrane ◽  
Yeast Cells ◽  
Ethanol Stress ◽  
Wild Type ◽  
Force Microscopy ◽  
Nanomechanical Properties ◽  
Atomic Force

ABSTRACTA wealth of biochemical and molecular data have been reported regarding ethanol toxicity in the yeastSaccharomyces cerevisiae. However, direct physical data on the effects of ethanol stress on yeast cells are almost nonexistent. This lack of information can now be addressed by using atomic force microscopy (AFM) technology. In this report, we show that the stiffness of glucose-grown yeast cells challenged with 9% (vol/vol) ethanol for 5 h was dramatically reduced, as shown by a 5-fold drop of Young's modulus. Quite unexpectedly, a mutant deficient in the Msn2/Msn4 transcription factor, which is known to mediate the ethanol stress response, exhibited a low level of stiffness similar to that of ethanol-treated wild-type cells. Reciprocally, the stiffness of yeast cells overexpressingMSN2was about 35% higher than that of the wild type but was nevertheless reduced 3- to 4-fold upon exposure to ethanol. Based on these and other data presented herein, we postulated that the effect of ethanol on cell stiffness may not be mediated through Msn2/Msn4, even though this transcription factor appears to be a determinant in the nanomechanical properties of the cell wall. On the other hand, we found that as with ethanol, the treatment of yeast with the antifungal amphotericin B caused a significant reduction of cell wall stiffness. Since both this drug and ethanol are known to alter, albeit by different means, the fluidity and structure of the plasma membrane, these data led to the proposition that the cell membrane contributes to the biophysical properties of yeast cells.IMPORTANCEEthanol is the main product of yeast fermentation but is also a toxic compound for this process. Understanding the mechanism of this toxicity is of great importance for industrial applications. While most research has focused on genomic studies of ethanol tolerance, we investigated the effects of ethanol at the biophysical level and found that ethanol causes a strong reduction of the cell wall rigidity (or stiffness). We ascribed this effect to the action of ethanol perturbing the cell membrane integrity and hence proposed that the cell membrane contributes to the cell wall nanomechanical properties.

scholarly journals FLO11Gene Is Involved in the Interaction of Flor Strains of Saccharomyces cerevisiae with a Biofilm-Promoting Synthetic Hexapeptide

2013 ◽  
Vol 79 (19) ◽  
pp. 6023-6032 ◽  
Author(s):  
Marc Bou Zeidan ◽  
Lourdes Carmona ◽  
Severino Zara ◽  
Jose F. Marcos
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Antimicrobial Peptides ◽  
Gene Knockout ◽  
Yeast Cells ◽  
Knockout Mutant ◽  
Fungal Cell ◽  
Content Type ◽  
Cell Penetrating ◽  
Flor Yeasts

ABSTRACTSaccharomyces cerevisiae“flor” yeasts have the ability to form a buoyant biofilm at the air-liquid interface of wine. The formation of biofilm, also called velum, depends onFLO11gene length and expression.FLO11encodes a cell wall mucin-like glycoprotein with a highly O-glycosylated central domain and an N-terminal domain that mediates homotypic adhesion between cells. In the present study, we tested previously known antimicrobial peptides with different mechanisms of antimicrobial action for their effect on the viability and ability to form biofilm ofS. cerevisiaeflor strains. We found that PAF26, a synthetic tryptophan-rich cationic hexapeptide that belongs to the class of antimicrobial peptides with cell-penetrating properties, but not other antimicrobial peptides, enhanced biofilm formation without affecting cell viability in ethanol-rich medium. The PAF26 biofilm enhancement required a functionalFLO11but was not accompanied by increasedFLO11expression. Moreover, fluorescence microscopy and flow cytometry analyses showed that the PAF26 peptide binds flor yeast cells and that aflo11gene knockout mutant lost the ability to bind PAF26 but not P113, a different cell-penetrating antifungal peptide, demonstrating that theFLO11gene is selectively involved in the interaction of PAF26 with cells. Taken together, our data suggest that the cationic and hydrophobic PAF26 hexapeptide interacts with the hydrophobic and negatively charged cell wall, favoring Flo11p-mediated cell-to-cell adhesion and thus increasing biofilm biomass formation. The results are consistent with previous data that point to glycosylated mucin-like proteins at the fungal cell wall as potential interacting partners for antifungal peptides.

scholarly journals Physiological and Transcriptional Responses of Saccharomyces cerevisiae tod-Limonene Show Changes to the Cell Wall but Not to the Plasma Membrane

2013 ◽  
Vol 79 (12) ◽  
pp. 3590-3600 ◽  
Author(s):  
Timothy C. R. Brennan ◽  
Jens O. Krömer ◽  
Lars K. Nielsen
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Plasma Membrane ◽  
Fatty Acid ◽  
Structural Integrity ◽  
Fatty Acid Biosynthesis ◽  
Membrane Integrity ◽  
Ethanol Exposure ◽  
Yeast Cells ◽  
Transcriptional Responses

ABSTRACTMonoterpenes can, upon hydrogenation, be used as light-fraction components of sustainable aviation fuels. Fermentative production of monoterpenes in engineered microorganisms, such asSaccharomyces cerevisiae, has gained attention as a potential route to deliver these next-generation fuels from renewable biomass. However, end product toxicity presents a formidable problem for microbial synthesis. Due to their hydrophobicity, monoterpene inhibition has long been attributed to membrane interference, but the molecular mechanism remains largely unsolved. In order to gain a better understanding of the mode of action, we analyzed the composition and structural integrity of the cell envelope as well as the transcriptional response of yeast cells treated with an inhibitory amount ofd-limonene (107 mg/liter). We found no alterations in membrane fluidity, structural membrane integrity, or fatty acid composition after the solvent challenge. A 4-fold increase in the mean fluorescence intensity per cell (using calcofluor white stain) and increased sensitivity to cell wall-degrading enzymes demonstrated that limonene disrupts cell wall properties. Global transcript measurements confirmed the membrane integrity observations by showing no upregulation of ergosterol or fatty acid biosynthesis pathways, which are commonly overexpressed in yeast to reinforce membrane rigidity during ethanol exposure. Limonene shock did cause a compensatory response to cell wall damage through overexpression of several genes (ROM1,RLM1,PIR3,CTT1,YGP1,MLP1,PST1, andCWP1) involved with the cell wall integrity signaling pathway. This is the first report demonstrating that cell wall, rather than plasma membrane, deterioration is the main source of monoterpene inhibition. We show that limonene can alter the structure and function of the cell wall, which has a clear effect on cytokinesis.

scholarly journals STUDIES ON THE OXIDATIVE METABOLISM OF SACCHAROMYCES CEREVISIAE

1961 ◽  
Vol 9 (3) ◽  
pp. 689-699 ◽  
Author(s):  
Eberhards Vitols ◽  
R. J. North ◽  
Anthony W. Linnane
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Single Unit ◽  
Osmium Tetroxide ◽  
Cytoplasmic Membrane ◽  
Yeast Cells ◽  
Unit Membrane ◽  
Animal Cells ◽  
Nuclear Pores ◽  
Thin Sections

Vegetative cells of Saccharomyces cerevisiae were fixed with potassium permanganate followed by uranyl nitrate, embedded in methacrylate, and studied in electron micrographs of thin sections. Details of the structure of the cell wall, cytoplasmic membrane, nucleus, vacuole, and mitochondria are described. Cell membranes, about 70 to 80 A thick, have been resolved into two dense layers, 20 to 25 A thick, separated by a light layer of the same dimensions, which correspond in thickness and appearance to the components of the "unit membrane" as described by Robertson (15). The cell wall is made up of zones of different electron opacity. Underlying the cell wall is the cytoplasmic membrane, a sinuous structure with numerous invaginations. The nucleoplasm, often of uneven electron opacity, is enclosed in a pair of unit membranes in which nuclear pores are apparent. The vacuole, limited by a single unit membrane, is usually irregular in outline and contains some dense material. Rod-shaped mitochondria, 0.4 to 0.6 µ in length and 0.2 to 0.3 µ in diameter, are smaller in size, but similar in structure to some of those described in plant and animal cells. Attempts to use osmium tetroxide as fixative were unsuccessful, a result similar to that obtained by other workers. It is suggested that yeast cells are impermeable to osmium tetroxide, except when grown under specific conditions.

Structural alteration of cell wall polysaccharides from Saccharomyces cerevisiae mutants

1988 ◽  
Vol 66 (3) ◽  
pp. 251-255 ◽  
Author(s):  
Tasuku Nakajima ◽  
Hiroshi Nishihara ◽  
Yogo Chiba ◽  
Kazuo Matsuda
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Structural Alteration ◽  
Cell Wall Polysaccharides
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