Molecular basis of mating in the yeast hansenula wingei

Crandall, Marjorie; Brock, Thomas D.

doi:10.1128/br.32.3.139-163.1968

Cited by 79 publications

(2 citation statements)

References 39 publications

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“…at the mating-type locus, and, lacking a better term, structural mannoproteins (Ballou, 1976). The external invertase of Saccharomyces cerevisiae (Gascon et al, 1968;Tarentino et al, 1974; Lehle et al, 1979) and the sexual agglutinins of Hansenula wingei (Crandall & Brock, 1968;Yen & Ballou, 1974;Burke et al, 1980) have been purified and analyzed in some detail, but little is known about the presumed structural mannoprotein other than what has been learned fortuitously from analyses performed on the total cell mannoprotein (Phaff, 1971; Ballou, 1976; Cohen et al, 1982).…”

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Saccharomyces cerevisiae structural cell wall mannoprotein

Frevert¹,

Ballou²

1985

Biochemistry

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A novel mannoprotein fraction with an average molecular weight of 180 000 has been isolated from Saccharomyces cerevisiae mnn9 mutant cell wall that was solubilized by beta-glucanase digestion. The same material could be extracted from purified wall fragments with 1% sodium dodecyl sulfate. The protein component, 12% by weight, is rich in proline, whereas the carbohydrate, mainly mannose, is about evenly distributed between asparagine and hydroxyamino acids. Endoglucosaminidase H digestion of the isolated mannoprotein reduced its average molecular weight to 150 000, but the mannoprotein, while still embedded in the cell wall, was inaccessible to the enzyme. Biosynthesis and translocation of the mannoprotein were investigated by following incorporation of [3H]proline into this fraction. In the presence of tunicamycin, both mnn9 and wild-type X2180 cells made a mannoprotein fraction with an average molecular weight of 140 000, whereas in the absence of the glycosylation inhibitor, the mnn9 mutant made material with a molecular weight of 180 000 and the mannoprotein made by wild-type cells was too large to penetrate the polyacrylamide gel. Although the cell wall mannoprotein was resistant to heat and proteolytic enzymes, attempts to isolate the carbohydrate-free component failed to yield any characteristic peptide material.

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Saccharomyces cerevisiae structural cell wall mannoprotein

Frevert¹,

Ballou²

1985

Biochemistry

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“…The 31P NMR spectrum of the Man3P showed it to be a mixture of a phos-IV^Iost yeast cell walls are composed of a fibrous glucan network interspersed with a matrix of mannoproteins of various types (Ballou, 1976). Among these extracellular glycoproteins are the enzymes invertase and acid phosphatase and macromolecules involved in sexual recognition and agglutination (Crandall & Brock, 1968). The latter are formed by haploid cells of perfect yeasts, and their synthesis is normally repressed in heterozygous diploids (Manney & Meade, 1977).…”

Section: Characterization Of Phosphorylated Oligomannosides From Hans...mentioning

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Characterization of phosphorylated oligomannosides from Hansenula wingei mannoprotein

Hashimoto¹,

Cohen²,

Ballou³

1980

Biochemistry

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Yeast cell wall mannoproteins often contain phosphate esterified to the oligosaccharide side chains, and partial acetolysis yields both neutral and phosphorylated fragments [Thieme, T. R., & Ballou, C. E. (1971) Biochemistry 10, 4121--4129]. We have isolated the acidic acetolysis fragments from Hansenula wingei mannoprotein [Yen, P. H., & Ballou, C. E. (1974) Biochemistry 13, 2420--2427] and have separated them into a mannopentaose monophosphate (Man5P) and a mannotriose monophosphate (Man3P). On the basis of selective enzymatic and partial acid hydrolysis and 1H and 31P NMR studies, Man5P was shown to have the structure P leads to 6 alpha Man1 leads to 3 alpha Man1 leads to 2 alpha Man1 leads to 2 alpha Man1 leads to 2Man (where Man = D-mannopyranose). The 31P NMR spectrum of the Man3P showed it to be a mixture of a phosphate monoester and a phosphate diester, which was separated by ion-exchange chromatography. The monoester had the structure P leads to 6 alpha Man1 leads to 3 alpha Man1 leads to 3Man whereas the diester had the properties of a cyclic phosphate. Although native H. wingei mannoprotein contains phosphodiester linkages, the starting mannoprotein preparation was isolated under alkaline conditions that hydrolyze such bonds, and it did not show a phosphodiester signal in the 31P NMR spectrum. We conclude that the cyclic phosphate was an artifact formed during the acetolysis reaction. Because acetolysis of H. wingei mannoprotein yields only phosphorylated mannotriose and mannopentaose whereas the mannoprotein contains mannotetraose side chains as well, the phosphorylation process must be a very specific event in the biosynthesis of the glycoprotein.

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Some Aspects of the Structure, Immunochemistry, and Genetic Control of Yeast Mannans

Ballou

1974

Advances in Enzymology - And Related Areas of Molecular Biology

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Molecular basis of mating in the yeast hansenula wingei

Cited by 79 publications

References 39 publications

Saccharomyces cerevisiae structural cell wall mannoprotein

Saccharomyces cerevisiae structural cell wall mannoprotein

Characterization of phosphorylated oligomannosides from Hansenula wingei mannoprotein

Some Aspects of the Structure, Immunochemistry, and Genetic Control of Yeast Mannans

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