Newly synthesised DNA of high molecular weight in the yeast Saccharomyces cerevisiae

1981 ◽  
Vol 3 (3) ◽  
pp. 229-233 ◽  
Author(s):  
Leland H. Johnston
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Molecular Weight ◽  
High Molecular Weight ◽  
Yeast Saccharomyces Cerevisiae

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.

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

PURIFICATION AND PROPERTIES OF AN INDUCIBLE β-GLUCOSIDASE OF BAKERS' YEAST

1966 ◽  
Vol 44 (8) ◽  
pp. 1099-1108 ◽  
Author(s):  
A. N. Inamdar ◽  
J. G. Kaplan
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Molecular Weight ◽  
Hydrolytic Activity ◽  
Chromogenic Substrate ◽  
Yeast Saccharomyces Cerevisiae ◽  
Intact Cells ◽  
Highly Active ◽  
Naturally Occurring ◽  
Purification And Properties ◽  
Competitive Inhibitors

The inducible β-glucosidase present in crude extracts of cellobiose-grown bakers' yeast (Saccharomyces cerevisiae C) was purified 50-fold and found to be homogeneous in the ultracentrifuge, with a molecular weight of 313,000. The enzyme was virtually identical in its properties with the internal, cryptic enzyme of the yeast cell, revealed by butanol treatment of the suspensions. It was unlike the membrane-localized enzyme found at the surface of intact cells in its low affinity for cellobiose and methyl-β-glucoside as substrates and inhibitors. The enzyme was specific for the β configuration and had no activity against substrates such as α-glucosides, β-galactosides, or β-xylosides. It was highly active against both naturally occurring and synthetic substrates with aromatic aglycones, and may thus be classed as an aryl-β-glucosidase. The enzyme had weak hydrolytic activity against methyl-β-glucoside and cellobiose, but these compounds, unlike all of the aryl-β-glucosides tested, were not competitive inhibitors of its activity against the chromogenic substrate pNPG. There were about 40,000 molecules of enzyme per cell in fully induced cultures and the enzyme represented about 3% of the total protein of these cells.

scholarly journals Apparent endocytosis of fluorescein isothiocyanate-conjugated dextran by Saccharomyces cerevisiae reflects uptake of low molecular weight impurities, not dextran.

1987 ◽  
Vol 105 (5) ◽  
pp. 1981-1987 ◽  
Author(s):  
R A Preston ◽  
R F Murphy ◽  
E W Jones
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Molecular Weight ◽  
Lucifer Yellow ◽  
Ph Dependence ◽  
Fluid Phase ◽  
Fluorescein Isothiocyanate ◽  
Low Molecular Weight ◽  
Yeast Saccharomyces Cerevisiae ◽  
Fluid Phase Endocytosis ◽  
Rapid Kinetics

Concurrent with Riezman's report (Riezman, H. 1985, Cell. 40:1001-1009) that fluid-phase endocytosis of the small molecule Lucifer yellow occurs in the yeast Saccharomyces cerevisiae, Makarow (Makarow, M. 1985. EMBO [Eur. Mol. Biol. Organ.] J. 4:1861-1866) reported the endocytotic uptake of 70-kD FITC-dextran (FD) and its subsequent compartmentation into the yeast vacuole. Samples of FD synthesized and purified here failed to label yeast vacuoles under conditions that allowed labeling using commercial FD. Chromatography revealed that the commercial FD was heavily contaminated with at least three low molecular weight fluorescent compounds. Dialysis was ineffective for removing the contaminants. After purification (Sephadex G25, ethanol extraction), commercial FD was incapable of labeling vacuoles. Extracts of cells labeled with partially purified FD contained FITC, not FD, based on Sephadex and thin layer chromatography. In either the presence or absence of unlabeled 70-kD dextran, authentic FITC (10 micrograms/ml) was an effective labeling agent for vacuoles. The rapid kinetics (0.28 pmol/min per 10(6) cells at pH 5.5) and the pH dependence of FITC uptake suggest that the mechanism of FITC uptake involves diffusion rather than endocytosis. In view of these results, labeling experiments that use unpurified commercial FD should be interpreted with caution.

scholarly journals Durable synthesis of high molecular weight heat shock proteins in G0 cells of the yeast and other eucaryotes.

1984 ◽  
Vol 99 (1) ◽  
pp. 199-207 ◽  
Author(s):  
H Iida ◽  
I Yahara
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Molecular Weight ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
High Molecular Weight ◽  
Resting State ◽  
Specific Class ◽  
Embryonic Fibroblasts ◽  
Long Period ◽  
Shock Proteins

We report that eucaryotic cells were induced to synthesize a specific class of heat shock proteins (hsps) when they entered the resting state, G0. This finding was originally made with Saccharomyces cerevisiae cells by taking advantage of the system in which we can distinguish between G1 arrests leading to G0 and those that do not result in G0 (Iida, H., and I. Yahara, 1984, J. Cell Biol. 98:1185-1193). Similar observations were subsequently made with higher eucaryotic cells including chick embryonic fibroblasts (CEF), mouse T lymphocytes, and Drosophila GM1 cells. The induction of hsps in G0 cells was distinct from that in heat-shocked cells in two respects. First, hsps with molecular weight around 25,000 were not induced in G0 cells, whereas most, if not all, high molecular weight (HMW) hsps were commonly induced both in G0 cells and in heat-shocked cells. Second, in contrast to the transient synthesis of hsps in heat-shocked cells, G0 cells continued to synthesize hsps at the stimulated rate for a relatively long period. These results suggest the possibility that high molecular weight hsps might function in a transition from the proliferating state to G0 or in maintaining G0 in the eucaryote.

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