title: Retention of Saccharomyces cerevisiae cell wall proteins through a phosphodiester-linked beta-1,3-/beta-1,6-glucan heteropolymer.
abstract: Yeast cell wall proteins, including Cwp1p and alpha-agglutinin, could be released by treating the cell wall with either beta-1,3-or beta-1,6-glucanases, indicating that both polymers are involved in anchoring cell wall proteins. It was shown immunologically that both beta-1,3- and beta-1,6-glucan were linked to yeast cell wall proteins, including Cwp1p and alpha-agglutinin. It was further shown that beta-1,3-glucan was linked to the wall protein through a beta-1,6-glucan moiety. The beta-1,6-glucan moiety could be removed from Cwp1p and other cell wall proteins by cleaving phosphodiester bridges either enzymatically using phosphodiesterases or chemically using ice-cold aqueous hydrofluoric acid. These observations are consistent with the notion that cell wall proteins in Saccharomyces cerevisiae are linked to a beta-1,3-/beta-1,6-glucan heteropolymer through a phosphodiester linkage and that this polymer is responsible for anchoring cell wall proteins. It is proposed that this polymer is identical to the alkali-soluble beta-1,3-/beta-1,6-glucan heteropolymer characterized by Fleet and Manners (1976, 1977).
authors.affiliation: Institute of Molecular Cell Biology, BioCentrum Amsterdam, University of Amsterdam, The Netherlands.
authors.forename: J C
authors.initials: JC
authors.lastname: Kapteyn
authors.forename: R C
authors.initials: RC
authors.lastname: Montijn
authors.forename: E
authors.initials: E
authors.lastname: Vink
authors.forename: J
authors.initials: J
authors.lastname: de la Cruz
authors.forename: A
authors.initials: A
authors.lastname: Llobell
authors.forename: J E
authors.initials: JE
authors.lastname: Douwes
authors.forename: H
authors.initials: H
authors.lastname: Shimoi
authors.forename: P N
authors.initials: PN
authors.lastname: Lipke
authors.forename: F M
authors.initials: FM
authors.lastname: Klis
mesh_terms: D001704:Biopolymers / Q000737:chemistry / Q000378:metabolism; D002236:Carbohydrate Conformation; D002473:Cell Wall / Q000737:chemistry / Q000378:metabolism*; D005656:Fungal Proteins / Q000378:metabolism*; D043326:Glucan 1,3-beta-Glucosidase; D005936:Glucans / Q000737:chemistry / Q000378:metabolism*; D006026:Glycoside Hydrolases; D000072235:Mating Factor; D008562:Membrane Glycoproteins / Q000737:chemistry / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism*; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins; D001617:beta-Glucosidase
chemical_list: D001704:Biopolymers; C093810:CWP1 protein, S cerevisiae; D005656:Fungal Proteins; D005936:Glucans; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D010455:Peptides; D029701:Saccharomyces cerevisiae Proteins; D000072235:Mating Factor; D006026:Glycoside Hydrolases; D001617:beta-Glucosidase; D043326:Glucan 1,3-beta-Glucosidase; C020105:endo-1,6-beta-glucanase