scholarly journals The structure of a β-(1→3)-d-glucan from yeast cell walls

1973 ◽  
Vol 135 (1) ◽  
pp. 19-30 ◽  
Author(s):  
David J. Manners ◽  
Alan J. Masson ◽  
James C. Patterson
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Molecular Weight ◽  
Yeast Cell ◽  
High Molecular Weight ◽  
Cell Walls ◽  
Minor Component ◽  
Yeast Saccharomyces Cerevisiae ◽  
Degree Of Branching ◽  
Degree Of Heterogeneity

Yeast glucan as normally prepared by various treatments of yeast (Saccharomyces cerevisiae) cell walls to remove mannan and glycogen is still heterogeneous. The major component (about 85%) is a branched β-(1→3)-glucan of high molecular weight (about 240000) containing 3% of β-(1→6)-glucosidic interchain linkages. The minor component is a branched β-(1→6)-glucan. A comparison of our results with those of other workers suggests that different glucan preparations may differ in the degree of heterogeneity and that the major β-(1→3)-glucan component may vary considerably in degree of branching.

scholarly journals The structure of a β-(1→6)-d-glucan from yeast cell walls

1973 ◽  
Vol 135 (1) ◽  
pp. 31-36 ◽  
Author(s):  
David J. Manners ◽  
Alan J. Masson ◽  
James C. Patterson ◽  
Håkan Björndal ◽  
Bengt Lindberg
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Yeast Cell ◽  
Cell Walls ◽  
Minor Component ◽  
Degree Of Polymerization ◽  
Chemical Fractionation ◽  
Yeast Saccharomyces Cerevisiae ◽  
A Minor ◽  
Branched Structure

By selective enzymolysis, or chemical fractionation, a minor polysaccharide component has been isolated from yeast (Saccharomyces cerevisiae) glucan. This minor component has a degree of polymerization of about 130–140, a highly branched structure, and a high proportion of β-(1→6)-glucosidic linkages. The molecules also contain a smaller proportion of β-(1→3)-glucosidic linkages that serve mainly as interchain linkages, but some may also be inter-residue linkages.

scholarly journals Characteristics of the Recovery of the Coenzyme A-Synthesizing Protein Complex from Saccharomyces Cerevisiae

1979 ◽  
Author(s):  
◽  
Stanley Tarnowski ◽  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Molecular Weight ◽  
Yeast Cell ◽  
Protein Complex ◽  
Coenzyme A ◽  
Pantothenic Acid ◽  
Exchange Chromatography ◽  
Yeast Cells ◽  
Multienzyme Complex ◽  
Yeast Saccharomyces Cerevisiae

A multienzyme complex contained in Bakers' yeast (Saccharomyces cerevisiae) which synthesizes CoA has been named the coenzyme A-synthesizing protein complex (CoA-SPC). The CoA-SPC has been shown to be insoluble in the crude Bakers' yeast cell lysate formed by exposing the yeast cell to ether and dry ice. Only after solubilization has this multienzyme complex been shown to catalyze the formation of bound dephospho-CoA utilizing the substrates adenosine triphosphate, D-pantothenic acid and L-cysteine. A low molecular weight component or components of the soluble fraction of the yeast cell and chloride ion appears to be responsible for the solubilization of CoA-SPC. This endogenous component of the yeast cell is referred to as t-Factor. Purification of t-Factor has been accomplished by techniques which have included dialysis, ultrafiltration and paper, permeation, adsorption and ion-exchange chromatography. Although the t-Factor has not been identified, several properties have been demonstrated: (1) the molecular weight is between 400 to 1,000; (2) it is stable to heat at 80°C for 24 hours; (3) it is resistant to hydrolysis by trypsin and protease; (4) it is inactivated by ashing; and (5) has no ultraviolet absorption at 260 mu and 280 my. Replacement of t-Factor by commercially available compounds or solubilizing agents has failed to reveal its identity. A "one-step" purification of CoA-SPC may be obtained by combining partially purified t-Factor with insoluble yeast cell residue. An alternate procedure was developed for the preparation of CoA-SPC. This procedure involves the slow drying and rehydration of the yeast cells, but the need for t-Factor still remains. Sonic oscillation and passage through a french pressure cell, two of the more classical cell breakage techniques, fail to produce active CoA-SPC preparations.

Accumulation of Polyphosphates and Expression of High Molecular Weight Exopolyphosphatase in the Yeast Saccharomyces cerevisiae

2005 ◽  
Vol 70 (9) ◽  
pp. 980-985 ◽  
Author(s):  
T. V. Kulakovskaya ◽  
N. A. Andreeva ◽  
L. V. Trilisenko ◽  
S. V. Suetin ◽  
V. M. Vagabov ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Molecular Weight ◽  
High Molecular Weight ◽  
Yeast Saccharomyces Cerevisiae

The 70-kilodalton adenylyl cyclase-associated protein is not essential for interaction of Saccharomyces cerevisiae adenylyl cyclase with RAS proteins

1992 ◽  
Vol 12 (11) ◽  
pp. 4937-4945
Author(s):  
J Wang ◽  
N Suzuki ◽  
T Kataoka
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Molecular Weight ◽  
Adenylyl Cyclase ◽  
High Molecular Weight ◽  
Size Difference ◽  
Missense Mutations ◽  
Ras Proteins ◽  
High Molecular Weight Complex ◽  
Ras Protein ◽  
Dependent Activity

In the yeast Saccharomyces cerevisiae, adenylyl cyclase is regulated by RAS proteins. We show here that the yeast adenylyl cyclase forms at least two high-molecular-weight complexes, one with the RAS protein-dependent adenylyl cyclase activity and the other with the Mn(2+)-dependent activity, which are separable by their size difference. The 70-kDa adenylyl cyclase-associated protein (CAP) existed in the former complex but not in the latter. Missense mutations in conserved motifs of the leucine-rich repeats of the catalytic subunit of adenylyl cyclase abolished the RAS-dependent activity, which was accompanied by formation of a very high molecular weight complex having the Mn(2+)-dependent activity. Contrary to previous results, disruption of the gene encoding CAP did not alter the extent of RAS protein-dependent activation of adenylyl cyclase, while a concomitant decrease in the size of the RAS-responsive complex was observed. These results indicate that CAP is not essential for interaction of the yeast adenylyl cyclase with RAS proteins even though it is an inherent component of the RAS-responsive adenylyl cyclase complex.

Extracting high molecular weight genomic DNA from Saccharomyces cerevisiae

2018 ◽  
Author(s):  
Erwan DENIS ◽  
Erwan Denis ◽  
Sophie Sanchez ◽  
Barbara Mairey ◽  
Odette Beluche ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Molecular Weight ◽  
High Molecular Weight ◽  
Genomic Dna

scholarly journals Cell fusion in yeast is negatively regulated by components of the cell wall integrity pathway

2019 ◽  
Vol 30 (4) ◽  
pp. 441-452 ◽  
Author(s):  
Allison E. Hall ◽  
Mark D. Rose
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Death ◽  
Cell Wall ◽  
Yeast Cell ◽  
Cell Fusion ◽  
Cell Walls ◽  
Cell Wall Integrity ◽  
Fusion Genes ◽  
Cell Wall Degradation ◽  
Cell Wall Integrity Pathway

During mating, Saccharomyces cerevisiae cells must degrade the intervening cell wall to allow fusion of the partners. Because improper timing or location of cell wall degradation would cause lysis, the initiation of cell fusion must be highly regulated. Here, we find that yeast cell fusion is negatively regulated by components of the cell wall integrity (CWI) pathway. Loss of the cell wall sensor, MID2, specifically causes “mating-induced death” after pheromone exposure. Mating-induced death is suppressed by mutations in cell fusion genes ( FUS1, FUS2, RVS161, CDC42), implying that mid2Δ cells die from premature fusion without a partner. Consistent with premature fusion, mid2Δ shmoos had thinner cell walls and lysed at the shmoo tip. Normally, Cdc42p colocalizes with Fus2p to form a focus only when mating cells are in contact (prezygotes) and colocalization is required for cell fusion. However, Cdc42p was aberrantly colocalized with Fus2p to form a focus in mid2Δ shmoos. A hyperactive allele of the CWI kinase Pkc1p ( PKC1*) caused decreased cell fusion and Cdc42p localization in prezygotes. In shmoos, PKC1* increased Cdc42p localization; however, it was not colocalized with Fus2p or associated with cell death. We conclude that Mid2p and Pkc1p negatively regulate cell fusion via Cdc42p and Fus2p.

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