Mannan structure analysis of the fragile Saccharomyces cerevisiae mutant VY1160

Maerkisch, Ulrich; Reuter, G.; Stateva, Lubomira; Venkov, Pencho

doi:10.1016/0020-711x(83)90029-0

Cited by 21 publications

(18 citation statements)

References 19 publications

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“…As shown in Table 1, S. cerevisiae 211 cells contained 51% protein and 7% nucleic acids. Its polysaccharide content (23%) was lower compared to other strains, which is due to the decreased contents of manoproteins and alkali-soluble glucan found in previous analytical determinations of cell wall components of the fragile S. cerevisiae mutants [15,16]. Unlike any other strain, however, S. cerevisiae 211 produced biomass with a very high degree of digestability.…”

Section: Composition Of the Yeast Subcellular Fractions And Potentialmentioning

confidence: 56%

Non-wasteful fractionation of fragile yeast cells for the production of nutritional protein and other by-products

Koleva

Stateva²,

Venkov³

1999

Zeitschrift f�r Lebensmitteluntersuchung und -Forschung A

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Saccharomyces cerevisiae 211 is a fragile yeast mutant whose cells grow only in media supplemented with osmotic stabilizer (1.6% NaCl), but which lyse spontaneously in water. This property provides a non-conventional way for isolation of nutritional protein and other products. We describe here a procedure based on the lysis ability of fragile yeasts for processing the biomass into several fractions. Cell lysis and downstream fractionation of the lysate do not include chemical or temperature treatment steps. The obtained protein fractions account for half of the starting biomass and contain 86% fully digestible protein and only 2% nucleic acids. The glycan fraction (with 83% polysaccharides) and the low molecular mass fraction are byproducts of the procedure. The latter can be used as a nutritional media supplement in microbiology and as a source for purification of 5b-GMP, a potent flavour enhancer. The high rate of quantitative recovery and the mild conditions used to fractionate the biomass indicate the advantages of the fragile yeasts for production of nutritional protein and other products on a large scale by an efficient and non-wasteful technology.

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Section: Composition Of the Yeast Subcellular Fractions And Potentialmentioning

confidence: 56%

Non-wasteful fractionation of fragile yeast cells for the production of nutritional protein and other by-products

Koleva

Stateva²,

Venkov³

1999

Zeitschrift f�r Lebensmitteluntersuchung und -Forschung A

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“…The srbl-J mutation (previous designation, srbl ; 15) has been found to produce defects in both the cell wall and the membrane. The walls of mutant cells contain less mannan than do those of the parent, and this mannan has an increased proportion of short side chains (17). The glucan structure of the walls of srbl-l mutants has also been found to be altered, being less branched in nature than that of the walls of the wild type (2a).…”

mentioning

confidence: 89%

Cloning and characterization of a gene which determines osmotic stability in Saccharomyces cerevisiae.

Stateva¹,

Oliver²,

Trueman³

et al. 1991

Mol. Cell. Biol.

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The srbl-1 mutation of Saccharomyces cerevisiae is an ochre allele which renders the yeast dependent on an osmotic stabilizer for growth and gives the cells the ability to lyse on transfer to hypotonic conditions. A DNA fragment which complements both of these phenotypic effects has been cloned. This clone contains a functional gene which is transcribed into a 2.3-kb polyadenylated mRNA molecule. Transformation of yeast strains carrying defined suppressible alleles demonstrated that the cloned fragment does not contain a nonsense suppressor. Integrative transformation and gene disruption experiments, when combined with classical genetic analysis, confirmed that the cloned fragment contained the wild-type SRB1 gene. The integrated marker was used to map SRB1 to chromosome XV by Southern hybridization and pulsed-field gel electrophoresis. A disruption mutant created by the insertion of a TRP1 marker into SRBI displayed only the lysis ability phenotype and was not dependent on an osmotic stabilizer for growth. Lysis ability was acquired by growth in (or transfer to) an osmotically stabilized environment, but only under conditions which permitted budding. It is inferred that budding cells lyse with a higher probability and that weak points in the wall at the site of budding are involved in the process. The biotechnological potential of the cloned gene and the disruption mutant is discussed. (15), and elevated levels of protein excretion (31). The srbl-J mutation (previous designation, srbl; 15) has been found to produce defects in both the cell wall and the membrane. The walls of mutant cells contain less mannan than do those of the parent, and this mannan has an increased proportion of short side chains (17). The glucan structure of the walls of srbl-l mutants has also been found to be altered, being less branched in nature than that of the walls of the wild type (2a). The pleiotropic effects of the mutation are not confined to the wall, however, since alterations in the lipid composition of the plasma membrane have also been observed (22b).It is not clear which of these effects is a direct consequence of the mutation and which is secondary in nature. Nevertheless, the range of effects suggests that the wild-type SRB1 gene encodes a protein which plays a major role in determining the structural integrity of the yeast cell. This, together with the practical utility of the mutant in the laboratory and its potential for the commercial production of yeast extracts (26,30), means that it is important to characterize the SRBI gene and identify its product. In this paper, we report the cloning and characterization of SRBI, as well as the construction by gene disruption of mutations which shed further light on its physiological role. MATERIALS AND METHODSStrains and media. The S. cerevisiae and Escherichia coli strains used in this study are listed in Table 1.The media used for the growth of yeast cells (YEPD, presporulation, sporulation, and selective dropout minimal media with appropriate combinations of amino acids or ...

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“…Work on strains carrying the srb1-1 mutation found a number of cell-wall changes, including alterations in glucan structure and composition (Blagoeva et al, 1991), and mannan content (Maerkisch et al, 1983). Investigations on the mode of action of actinomycin D (Waltschewa et al, 1976) and rifampicin (Venkov et al, 1975) have been facilitated by the hypersensitivity to antibiotics shown by strains carrying the srb1-1 mutation.…”

Section: Psa1-leu2mentioning

confidence: 99%

“…Additional phenotypes include the ability to lyse upon hypotonic shock, antibiotic hypersensitivity and increased permeability of the cell wall and membrane due to defects in their structure and composition (Maerkisch et al, 1983 ;Blagoeva et al, 1991 ;Kopecka et al, 1991). In a previous study (Stateva et al, 1991), a yeast chromosomal gene was isolated that complemented sorbitol dependence in a number of srb strains, including 4STLU.…”

Section: Psa1/vig9 Encoding Gdp-mannose Pyrophosphorylase Is the Bomentioning

confidence: 99%

Suppression of sorbitol dependence in a strain bearing a mutation in the SRB1/PSA1/VIG9 gene encoding GDP-mannose pyrophosphorylase by PDE2 overexpression suggests a role for the Ras/cAMP signal-transduction pathway in the control of yeast cell-wall biogenesis

et al. 2000

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Complementation studies and allele replacement in Saccharomyces cerevisiae revealed that PSA1/VIG9, an essential gene that encodes GDP-mannose pyrophosphorylase, is the wild-type SRB1 gene. Cloning and sequencing of the srb1-1 allele showed that it determines a single amino acid change from glycine to aspartic acid at residue 276 (srb1 D276 ). Genetic evidence is presented showing that at least one further mutation is required for the sorbitol dependence of srb1 D276 . A previously reported complementing gene, which this study has now identified as PDE2, is a multi-copy suppressor of sorbitol dependence and is not, as was previously suggested, the SRB1 gene. srb and pde2 mutants share a number of phenotypes, including lysis upon hypotonic shock and enhanced transformability. These data are consistent with the idea that the Ras/cAMP pathway might modulate cell-wall construction.

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Mannan structure analysis of the fragile Saccharomyces cerevisiae mutant VY1160

Cited by 21 publications

References 19 publications

Non-wasteful fractionation of fragile yeast cells for the production of nutritional protein and other by-products

Non-wasteful fractionation of fragile yeast cells for the production of nutritional protein and other by-products

Cloning and characterization of a gene which determines osmotic stability in Saccharomyces cerevisiae.

Suppression of sorbitol dependence in a strain bearing a mutation in the SRB1/PSA1/VIG9 gene encoding GDP-mannose pyrophosphorylase by PDE2 overexpression suggests a role for the Ras/cAMP signal-transduction pathway in the control of yeast cell-wall biogenesis

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