Comparison of β-Glucan Structures in a Cell Wall Mutant of Saccharomyces cerevisiae and the Wild Type

Shiota, Masao; Nakajima, Tasuku; Satoh, Akiko; Shida, Mariko; Matsuda, Kazuo

doi:10.1093/oxfordjournals.jbchem.a135397

Cited by 21 publications

(9 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We have not precisely analyzed the nature of the linkages of the P-glucan fractions from the mutant strains; therefore, we cannot rule out the possibility that small changes in the length of the (1-3)p-linked glucose chains or small differences in the degree of (1-6)p crosslinking possibly affect the secondary and tertiary conformation of the 3-glucan and, ultimately, the nature of the network structure in the cell wall and the shape of the cell. In fact, some authors (11,28) favor the hypothesis that the number of (1-6)1-glycosidic linkages is a key element in controlling the hydrodynamic properties and morphology of the yeast cell wall. Indeed, very recently (1,18) Bussey and coworkers clearly showed the role of (1-6),B-D-glucan in cell morphology and cell growth in S. cerevisiae.…”

Section: Discussionmentioning

confidence: 99%

“…In fact, some important studies have been performed with S. cerevisiae mutants altered in the biosynthesis of other cell wall polymers such as mannan (4,15) or chitin (2,29). Although P-D-glucan is assumed to be essential for yeast cell integrity, very few studies have been done with ,B-glucan mutants (11,20,28), and most of them refer to the (1-6),3-D-glucan from S. cerevisiae. A recent study of KRE genes, involved in killer factor resistance (1,18), has provided the first evidence for a pathway of (1-6)-p-D-glucan synthesis and cell wall ,3-glucan assembly in S. cerevisiae.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Isolation and characterization of Schizosaccharomyces pombe mutants defective in cell wall (1-3)beta-D-glucan

et al. 1991

View full text Add to dashboard Cite

Schizosaccharomyces pombe thermosensitive mutants requiring the presence of an osmotic stabilizer to survive and grow at a nonpermissive temperature were isolated. The mutants were genetically and biochemically characterized. In all of them, the phenotype segregated in Mendelian fashion as a single gene which coded for a recessive character. Fourteen loci were defined by complementation analysis. Studies of cell wall composition showed a reduction in the amount of cell wall ,I-glucan in three strains (JCR1, JCR5, and JCR10) when growing at 37°C. Galactomannan was diminished in two others. Strains JCR1 and JCR5, with mutant alleles cwgl-l and cwg2-1, respectively, were further studied. The cwgl locus was mapped on the right arm of chromosome III, 18.06 centimorgans (cM) to the left of the ade5 marker; cwg2 was located on the left arm of chromosome I, 34.6 cM away from the aroS marker. (1-3)0-D-Glucan synthase activities from cwgl-l and cwg2-1 mutant strains grown at 37°C were diminished, as measured in vitro, compared with the wild-type strain; however, Km values and activation by GTP were similar to the wild-type values. Mutant synthases behaved like the wild-type enzyme in terms of thermostability. Analyses of round shape, lytic behavior, and low (1-3)0-D-glucan synthase activity in cultures derived from ascospores of the same tetrad showed cosegregation of all these characters. Detergent dissociation of (1-3)01-D-glucan synthase into soluble and particulate fractions and subsequent reconstitution demonstrated that the cwgl-1 mutant was affected in the particulate fraction of the enzymatic activity while cwg2-1 was affected in the soluble component. The antifungal agents Papulacandin B and Aculeacin A had similar effects on the enzymatic activities of the wild type and the cwg2-1 mutant strain, whereas the cwgl-1 mutant, when growing at 37°C, had a more inhibitor-resistant (1-3)0-D-glucan synthase. It is concluded that the cwgl+ and cwg2+ genes are related to (1-3)0I-D-glucan biosynthesis.

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Isolation and characterization of Schizosaccharomyces pombe mutants defective in cell wall (1-3)beta-D-glucan

et al. 1991

View full text Add to dashboard Cite

show abstract

“…In fact, only a few linear (1 6)-β-glucans have been identified, the best known being pustulan from Umbilicaria species [2] and lutean from Penicillium luteum [3]. However, (1 6)-β-linkages occur frequently in the glucans of yeast and filamentous-fungal cell walls [4][5][6][7][8][9] and, not surprisingly, enzymes hydrolysing (1 6)-β-glucosidic linkages are common in these organisms [10][11][12][13].…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of an extracellular (1 → 6)-β-glucanase from the filamentous fungus Acremonium persicinum

Pitson

Seviour

McDougall

et al. 1996

Biochemical Journal

View full text Add to dashboard Cite

An endo-(1 --> 6)-beta-glucanase has been isolated from the culture filtrates of the filamentous fungus Acremonium persicinum and purified by (NH4)2SO4 precipitation followed by anion-exchange and gel-filtration chromatography. SDS/PAGE of the purified enzyme gave a single band with an apparent molecular mass of 42.7 kDa. The enzyme is a non-glycosylated, monomeric protein with a pI of 4.9 and pH optimum of 5.0. It hydrolysed (1 --> 6)-beta-glucans (pustulan and lutean), initially yielding a series of (1 --> 6)-beta-linked oligoglucosides, consistent with endo-hydrolytic action. Final hydrolysis products from these substrates were gentiobiose and gentiotriose, with all products released as beta-anomers, indicating that the enzyme acts with retention of configuration. The purified enzyme also hydrolysed Eisenia bicyclis laminarin, liberating glucose, gentiobiose, and a range of larger oligoglucosides, through the apparent bydrolysis of (1 --> 6)-beta- and some (1 --> 3)-beta-linkages in this substrate. K(m) values for pustulan, lutean and laminarin were 1.28, 1.38, and 1.67 mg/ml respectively. The enzyme was inhibited by N-acetylimidazole, N-bromosuccinimide, dicyclohexylcarbodi-imide, Woodward's Reagent K, 2-hydroxy-5-nitrobenzyl bromide, KMnO4 and some metal ions, whereas D-glucono-1,5-lactone and EDTA had no effect.

show abstract

“…Genes that are involved in (1,3)-3-glucan synthesis, however, remain largely unknown. Enzymatic studies revealed that the (1,3)-p-glucan synthase is likely to be a membrane-associated protein regulated by a G protein (11,30), and mutants with reduced levels of (1,3)-p-glucan have been isolated and characterized (28,48,57). We report here the cloning and characterization ofKNR4, a gene involved in (1,3)-,B-glucan biosynthesis.…”

mentioning

confidence: 97%

Cloning and characterization of KNR4, a yeast gene involved in (1,3)-beta-glucan synthesis.

Hong¹,

Mann²,

Brown³

et al. 1994

Mol. Cell. Biol.

View full text Add to dashboard Cite

k9 killer toxin from Hansenula mrakii was used to select a number of resistant mutants from Saccharomyces cerevisiae. Preliminary biochemical and genetic studies showed that some of them acquired structural defects in the cell wall. One of these mutants, the knr4-1 mutant, displays a number of cell wall defects, including osmotic sensitivity; sensitivity to cercosporamide, a known antifungal agent; and resistance to Zymolyase, a (1,3)-beta-glucanase. We report here the isolation and analysis of the KNR4 gene. DNA sequence analysis revealed an uninterrupted open reading frame which contains five potential start codons. The longest coding template encodes a protein of 505 amino acids with a calculated molecular mass of 57,044 Da. A data base search revealed 100% identity with a nuclear protein, SMI1p. Disruption of the KNR4 locus does not result in cell death; however, it leads to reduced levels of both (1,3)-beta-glucan synthase activity and (1,3)-beta-glucan content in the cell wall. The gene was mapped to the right arm of chromosome VII.

show abstract

Comparison of β-Glucan Structures in a Cell Wall Mutant of Saccharomyces cerevisiae and the Wild Type

Cited by 21 publications

References 0 publications

Isolation and characterization of Schizosaccharomyces pombe mutants defective in cell wall (1-3)beta-D-glucan

Isolation and characterization of Schizosaccharomyces pombe mutants defective in cell wall (1-3)beta-D-glucan

Purification and characterization of an extracellular (1 → 6)-β-glucanase from the filamentous fungus Acremonium persicinum

Cloning and characterization of KNR4, a yeast gene involved in (1,3)-beta-glucan synthesis.

Contact Info

Product

Resources

About