Glucomannoproteins in the cell wall of Saccharomyces cerevisiae contain a novel type of carbohydrate side chain.

Montijn, R.C.; Rinsum, J Van; Schagen, F A van; Klis, Frans M.

doi:10.1016/s0021-9258(17)32172-5

Cited by 119 publications

(13 citation statements)

References 15 publications

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“…Like Ag 1p, other CWPs could be released from the cell wall by 1,3-glucanases. These proteins were shown to contain 1,6-glucan (Montijn et al, 1994;Van Berkel et al, 1994;Van Der Vaart et al, 1995Kapteyn et al, 1996). From these proteins, the 1,6-glucan could be released by treatment with aqueous HF, which is known to cleave phosphodiester bonds, suggesting that 1,6-glucan is attached to the GPI-anchor remnant (Kapteyn et al, 1996).…”

Section: Discussionmentioning

confidence: 99%

In silicio identification of glycosyl-phosphatidylinositol-anchored plasma-membrane and cell wall proteins ofSaccharomyces cerevisiae

Caro

Tettelin

Vossen

et al. 1997

Yeast

316

325

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Use of the Von Heijne algorithm allowed the identification of 686 open reading frames (ORFs) in the genome of Saccharomyces cerevisiae that encode proteins with a potential N-terminal signal sequence for entering the secretory pathway. On further analysis, 51 of these proteins contain a potential glycosyl-phosphatidylinositol (GPI)attachment signal. Seven additional ORFs were found to belong to this group. Upon examination of the possible GPI-attachment sites, it was found that in yeast the most probable amino acids for GPI-attachment are asparagine and glycine.In yeast, GPI-proteins are found at the cell surface, either attached to the plasma-membrane or as an intrinsic part of the cell wall. It was noted that plasma-membrane GPI-proteins possess a dibasic residue motif just before their predicted GPI-attachment site. Based on this, and on homologies between proteins, families of plasma-membrane and cell wall proteins were assigned, revealing 20 potential plasma-membrane and 38 potential cell wall proteins. For members of three plasma-membrane protein families, a function has been described. On the other hand, most of the cell wall proteins seem to be structural components of the wall, responsive to different growth conditions.The GPI-attachment site of yeast slightly differs from mammalian cells. This might be of use in the development of anti-fungal drugs. 1997 John Wiley & Sons, Ltd.

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Section: Discussionmentioning

confidence: 99%

In silicio identification of glycosyl-phosphatidylinositol-anchored plasma-membrane and cell wall proteins ofSaccharomyces cerevisiae

Caro

Tettelin

Vossen

et al. 1997

Yeast

316

325

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“…The anti-/~l,6-glucan antiserum was raised against bovine serum albumin-/~l,6-glucan conjugates in rabbit (Montijn et al, 1994) and was purified using affinity chromatography. Epoxy-activated Sepharose 6B (Pharmacia Fine Chemicals, Piscataway, NJ) was used to couple B1,6-glucan via direct coupling of free oxirane groups to the hydroxyl groups of the sugars.…”

Section: Purification Of Anti-fjl6-glucan Antibodiesmentioning

confidence: 99%

“…Molecular Size of Cell Wall ~-Agglutinin Some/31,3-glucanase-extractable cell wall proteins are covalently linked to/$1,6-glucans (Montijn et al, 1994). We speculated that the cell wall anchorage of ot-agglutinin resulted from a covalent linkage to the wall fll,6-glucan which was in turn cross-linked to other cell wall components.…”

Section: Kre Mutations Affect Cell Wall Anchorage Andmentioning

confidence: 99%

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Glycosyl phosphatidylinositol-dependent cross-linking of alpha-agglutinin and beta 1,6-glucan in the Saccharomyces cerevisiae cell wall.

Montijn

Brown

et al. 1995

The Journal of Cell Biology

196

187

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Abstract. The cell adhesion protein t~-agglutinin is bound to the outer surface of the Saccharomyces cerevisiae cell wall and mediates cell-cell contact in mating, a-Agglutinin is modified by addition of a glycosyl phosphatidylinositol (GPI) anchor as it traverses the secretory pathway. The presence of a GPI anchor is essential for cross-linking into the wall, but the fatty acid and inositol components of the anchor are lost before cell wall association (Lu, C.-E, J. Kurjan, and P. N. . A pathway for cell wall anchorage of Saccharomyces cerevisiae a-agglutinin. Mol. . Cell wall association of ot-agglutinin was accompanied by an increase in size and a gain in reactivity to antibodies directed against ~l,6-glucan. Several kre mutants, which have defects in synthesis of cell wall/~l,6-glucan, had reduced molecular size of cell wall ot-agglutinin. These findings demonstrate that the cell wall form of oz-agglutinin is covalently associated with/31,6-glucan. The ot-agglutinin biosynthetic precursors did not react with antibody to/~l,6-glucan, and the sizes of these forms were unaffected in kre mutants. A COOHterminal truncated form of a-agglutinin, which is not GPI anchored and is secreted into the medium, did not react with the anti-/31,6-glucan. We propose that extracellular cross-linkage to/31,6-glucan mediates covalent association of a-agglutinin with the cell wall in a manner that is dependent on prior addition of a GPI anchor to ot-agglutinin.

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“…A part of these proteins is simply adsorbed non-covalently to β-1,3-glucan [10], while the others are linked covalently. Of the latter, most proteins migrate along the secretory pathway to the plasma membrane in a GPI-anchored form and are then translocated to preformed β-1,6-glucan molecules attached to the β-1,3-glucan network [11,12]. A smaller group of non-GPI bound proteins comprise mostly Pir-proteins covalently attached to β-1,3-glucan through ester bonds created by particular glutamines located in a specific repeating motif at the N-terminal part of the protein [13].…”

Section: Introductionmentioning

confidence: 99%

Systematic Comparison of Cell Wall-Related Proteins of Different Yeasts

Lozančić

Žunar

Hrestak

et al. 2021

JoF

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Yeast cell walls have two major roles, to preserve physical integrity of the cell, and to ensure communication with surrounding molecules and cells. While the first function requires evolutionary conserved polysaccharide network synthesis, the second needs to be flexible and provide adaptability to different habitats and lifestyles. In this study, the comparative in silico analysis of proteins required for cell wall biosynthesis and functions containing 187 proteins of 92 different yeasts was performed in order to assess which proteins were broadly conserved among yeasts and which were more species specific. Proteins were divided into several groups according to their role and localization. As expected, many Saccharomyces cerevisiae proteins involved in protein glycosylation, glycosylphosphatidylinositol (GPI) synthesis and the synthesis of wall polysaccharides had orthologues in most other yeasts. Similarly, a group of GPI anchored proteins involved in cell wall biosynthesis (Gas proteins and Dfg5p/Dcw1p) and other non-GPI anchored cell wall proteins involved in the wall synthesis and remodeling were highly conserved. However, GPI anchored proteins involved in flocculation, aggregation, cell separation, and those of still unknown functions were not highly conserved. The proteins localized in the cell walls of various yeast species were also analyzed by protein biotinylation and blotting. Pronounced differences were found both in the patterns, as well as in the overall amounts of different groups of proteins. The amount of GPI-anchored proteins correlated with the mannan to glucan ratio of the wall. Changes of the wall proteome upon temperature shift to 42 °C were detected.

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Glucomannoproteins in the cell wall of Saccharomyces cerevisiae contain a novel type of carbohydrate side chain.

Cited by 119 publications

References 15 publications

In silicio identification of glycosyl-phosphatidylinositol-anchored plasma-membrane and cell wall proteins ofSaccharomyces cerevisiae

In silicio identification of glycosyl-phosphatidylinositol-anchored plasma-membrane and cell wall proteins ofSaccharomyces cerevisiae

Glycosyl phosphatidylinositol-dependent cross-linking of alpha-agglutinin and beta 1,6-glucan in the Saccharomyces cerevisiae cell wall.

Systematic Comparison of Cell Wall-Related Proteins of Different Yeasts

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