Saccharomyces cerevisiae accumulates GAPDH-derived peptides on its cell surface that induce death of non-Saccharomyces yeasts by cell-to-cell contact

alpha-Agglutinin is a cell adhesion glycoprotein expressed on the cell wall of Saccharomyces cerevisiae alpha cells. Binding of alpha-agglutinin to its ligand a-agglutinin, expressed by a cells, mediates cell-cell contact during mating. Analysis of truncations of the 650-amino-acid alpha-agglutinin structural gene AG alpha 1 delineated functional domains of alpha-agglutinin. Removal of the C-terminal hydrophobic sequence allowed efficient secretion of the protein and loss of cell surface attachment. This cell surface anchorage domain was necessary for linkage to a glycosyl phosphatidylinositol anchor. A construct expressing the N-terminal 350 amino acid residues retained full a-agglutinin-binding activity, localizing the binding domain to the N-terminal portion of alpha-agglutinin. A 278-residue N-terminal peptide was inactive; therefore, the binding domain includes residues between 278 and 350. The segment of alpha-agglutinin between amino acid residues 217 and 308 showed significant structural and sequence similarity to a consensus sequence for immunoglobulin superfamily variable-type domains. The similarity of the alpha-agglutinin-binding domain to mammalian cell adhesion proteins suggests that this structure is a highly conserved feature of adhesion proteins in diverse eukaryotes.

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Cell surface anchorage and ligand-binding domains of the Saccharomyces cerevisiae cell adhesion protein alpha-agglutinin, a member of the immunoglobulin superfamily

Molecular and Cellular Biology ◽

10.1128/mcb.13.4.2554-2563.1993 ◽

1993 ◽

Vol 13 (4) ◽

pp. 2554-2563

Author(s):

D Wojciechowicz ◽

C F Lu ◽

J Kurjan ◽

P N Lipke

Keyword(s):

Saccharomyces Cerevisiae ◽

Cell Adhesion ◽

Amino Acid ◽

Cell Surface ◽

Consensus Sequence ◽

Binding Domain ◽

Immunoglobulin Superfamily ◽

Cell Contact ◽

Amino Acid Residues ◽

Adhesion Proteins

alpha-Agglutinin is a cell adhesion glycoprotein expressed on the cell wall of Saccharomyces cerevisiae alpha cells. Binding of alpha-agglutinin to its ligand a-agglutinin, expressed by a cells, mediates cell-cell contact during mating. Analysis of truncations of the 650-amino-acid alpha-agglutinin structural gene AG alpha 1 delineated functional domains of alpha-agglutinin. Removal of the C-terminal hydrophobic sequence allowed efficient secretion of the protein and loss of cell surface attachment. This cell surface anchorage domain was necessary for linkage to a glycosyl phosphatidylinositol anchor. A construct expressing the N-terminal 350 amino acid residues retained full a-agglutinin-binding activity, localizing the binding domain to the N-terminal portion of alpha-agglutinin. A 278-residue N-terminal peptide was inactive; therefore, the binding domain includes residues between 278 and 350. The segment of alpha-agglutinin between amino acid residues 217 and 308 showed significant structural and sequence similarity to a consensus sequence for immunoglobulin superfamily variable-type domains. The similarity of the alpha-agglutinin-binding domain to mammalian cell adhesion proteins suggests that this structure is a highly conserved feature of adhesion proteins in diverse eukaryotes.

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Faculty Opinions recommendation of Cell contact-dependent immunosuppression by CD4(+)CD25(+) regulatory T cells is mediated by cell surface-bound transforming growth factor beta.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1000961.10054 ◽

2002 ◽

Author(s):

Bruce Blazar

Keyword(s):

T Cells ◽

Growth Factor ◽

Regulatory T Cells ◽

Cell Surface ◽

Transforming Growth Factor Beta ◽

Transforming Growth Factor ◽

Cell Contact ◽

Growth Factor Beta

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The AGA1 product is involved in cell surface attachment of the Saccharomyces cerevisiae cell adhesion glycoprotein a-agglutinin.

Molecular and Cellular Biology ◽

10.1128/mcb.11.8.4196 ◽

1991 ◽

Vol 11 (8) ◽

pp. 4196-4206 ◽

Cited By ~ 106

Author(s):

A Roy ◽

C F Lu ◽

D L Marykwas ◽

P N Lipke ◽

J Kurjan

Keyword(s):

Saccharomyces Cerevisiae ◽

Cell Surface ◽

Signal Sequence ◽

Complementation Group ◽

Alpha Cells ◽

Specific Expression ◽

Surface Attachment ◽

Cellular Aggregation ◽

Specific Regulation ◽

Binding Subunit

Saccharomyces cerevisiae a and alpha cells express the complementary cell surface glycoproteins a-agglutinin and alpha-agglutinin, respectively, which interact with one another to promote cellular aggregation during mating. Treatment of S. cerevisiae a cells with reducing agents releases the binding subunit of a-agglutinin, which has been purified and characterized; little biochemical information on the overall structure of a-agglutinin is available. To characterise a-agglutinin structure and function, we have used a genetic approach to clone an a-agglutinin structural gene (AGAI). Mutants with a-specific agglutination defects were isolated, the majority of which fell into a single complementation group, called aga1. The aga1 mutants showed wild-type pheromone production and response, efficient mating on solid medium, and a mating defect in liquid medium; these phenotypes are characteristic of agglutinin mutants. The AGA1 gene was cloned by complementation; the gene sequence indicated that it could encode a protein of 725 amino acids with high serine and threonine content, a putative N-terminal signal sequence, and a C-terminal hydrophobic sequence similar to signals for the attachment to glycosyl phosphatidylinositol anchors. Active a-agglutinin binding subunit is secreted by aga1 mutants, indicating that AGA1 is involved in cells surface attachment of a-agglutinin. This result suggests that AGA1 encodes a protein with functional similarity to the core subunits of a-agglutinin analogs from other budding yeasts. Unexpectedly, the AGA1 transcript was expressed and induced by pheromone in both a and alpha cells, suggesting that the a-specific expression of active a-agglutinin results only from a-specific regulation of the a-agglutinin binding subunit.

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Chemical modifications of the cell-surface components of Lactobacillus fermentum FTPT 1405 and their effect on the flocculation of Saccharomyces cerevisiae

World Journal of Microbiology and Biotechnology ◽

10.1007/bf00286363 ◽

1995 ◽

Vol 11 (5) ◽

pp. 508-511

Author(s):

R. Bromberg ◽

F. Yokoya

Keyword(s):

Saccharomyces Cerevisiae ◽

Cell Surface ◽

Lactobacillus Fermentum ◽

Chemical Modifications

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Remodeling the cell surface distribution of membrane proteins during the development of epithelial cell polarity.

The Journal of Cell Biology ◽

10.1083/jcb.116.4.889 ◽

1992 ◽

Vol 116 (4) ◽

pp. 889-899 ◽

Cited By ~ 60

Author(s):

D A Wollner ◽

K A Krzeminski ◽

W J Nelson

Keyword(s):

Epithelial Cell ◽

Membrane Proteins ◽

Cell Surface ◽

Mdck Cells ◽

Apical Cell ◽

Cell Contact ◽

Surface Polarity ◽

Lateral Membrane ◽

E Cadherin ◽

Cell Cell

The development of polarized epithelial cells from unpolarized precursor cells follows induction of cell-cell contacts and requires resorting of proteins into different membrane domains. We show that in MDCK cells the distributions of two membrane proteins, Dg-1 and E-cadherin, become restricted to the basal-lateral membrane domain within 8 h of cell-cell contact. During this time, however, 60-80% of newly synthesized Dg-1 and E-cadherin is delivered directly to the forming apical membrane and then rapidly removed, while the remainder is delivered to the basal-lateral membrane and has a longer residence time. Direct delivery of greater than 95% of these proteins from the Golgi complex to the basal-lateral membrane occurs greater than 48 h later. In contrast, we show that two apical proteins are efficiently delivered and restricted to the apical cell surface within 2 h after cell-cell contact. These results provide insight into mechanisms involved in the development of epithelial cell surface polarity, and the establishment of protein sorting pathways in polarized cells.

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Role of cations in the flocculation of Saccharomyces cerevisiae and discrimination of the corresponding proteins

Canadian Journal of Microbiology ◽

10.1139/m91-064 ◽

1991 ◽

Vol 37 (5) ◽

pp. 397-403 ◽

Cited By ~ 17

Author(s):

Hiroshi Kuriyama ◽

Itaru Umeda ◽

Harumi Kobayashi

Keyword(s):

Saccharomyces Cerevisiae ◽

Cell Surface ◽

Inhibitory Effect ◽

Surface Proteins ◽

Promoting Effect ◽

Yeast Strains ◽

Yeast Flocculation ◽

Different Types ◽

Anionic Groups

Asexual yeast flocculation was studied using strong flocculents of Saccharomyces cerevisiae. The inhibitory effect of cations on flocculation is considered to be caused by competition between those cations and Ca2+ at the binding site of the Ca2+-requiring protein that is involved in flocculation. Inhibition of flocculation by various cations occurred in the following order: La3+, Sr2+, Ba2+, Mn2+, Al3+, and Na+. Cations such as Mg2+, Co2+, and K+ promoted flocculation. This promoting effect may be based on the reduction of electrostatic repulsive force between cells caused by binding of these cations anionic groups present on the cell surface. In flocculation induced by these cations, trace amounts of Ca2+ excreted on the cell surface may activate the corresponding protein. The ratio of Sr2+/Ca2+ below which cells flocculated varied among strains: for strains having the FLO5 gene, it was 400 to 500; for strains having the FLO1 gene, about 150; and for two alcohol yeast strains, 40 to 50. This suggests that there are several different types of cell surface proteins involved in flocculation in different yeast strains. Key words: yeast, flocculation, protein, cation, calcium.

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Studies of membrane fusion. I. Paramyxovirus-induced cell fusion, a scanning electron-microscope study

Journal of Cell Science ◽

10.1242/jcs.28.1.179 ◽

1977 ◽

Vol 28 (1) ◽

pp. 179-188

Author(s):

S. Knutton ◽

D. Jackson ◽

M. Ford

Keyword(s):

Cell Surface ◽

Cell Fusion ◽

Hela Cells ◽

Cell Swelling ◽

Cell Contact ◽

Cell Agglutination ◽

Scanning Electron Microscope Study ◽

Virus Particles ◽

Scanning Electron ◽

Cell Cell

Fusion of erythrocytes and HeLa cells with Sendai and Newcastle disease viruses has been studied by scanning electron microscopy. Most virus particles are spherical but vary in diameter from approximately 200 to approximately 600 nm. At 4 degrees C virus particles bind randomly to the cell surface and at high cell densities cross-linking of adjacent cells by virus particles results in cell agglutination. Cell-cell fusion takes place when the agglutinated cell suspension is warmed to 37 degrees C. Fusion is initiated at sites of cell-cell contact and is accompanied in all cases by cell swelling. In the case of suspension HeLa cells, virally mediated cell swelling involves an ‘unfolding’ of cell surface microvilli and results in the formation of smooth-surfaced single or fused cells. With erythrocytes, swelling results in haemolysis. There is a dramatic reduction in the numbers of virus particles bound to cells following fusion.

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Quantitation of alpha-factor internalization and response during the Saccharomyces cerevisiae cell cycle

Molecular and Cellular Biology ◽

10.1128/mcb.11.10.5251-5258.1991 ◽

1991 ◽

Vol 11 (10) ◽

pp. 5251-5258

Author(s):

B Zanolari ◽

H Riezman

Keyword(s):

Saccharomyces Cerevisiae ◽

Cell Cycle ◽

Cell Surface ◽

Cell Surface Receptors ◽

Specific Cell ◽

Surface Receptors ◽

Cycle Arrest ◽

A Cells ◽

Alpha Factor ◽

Inducible Genes

The alpha-factor pheromone binds to specific cell surface receptors on Saccharomyces cerevisiae a cells. The pheromone is then internalized, and cell surface receptors are down-regulated. At the same time, a signal is transmitted that causes changes in gene expression and cell cycle arrest. We show that the ability of cells to internalize alpha-factor is constant throughout the cell cycle, a cells are also able to respond to pheromone throughout the cycle even though there is cell cycle modulation of the expression of two pheromone-inducible genes, FUS1 and STE2. Both of these genes are expressed less efficiently near or just after the START point of the cell cycle in response to alpha-factor. For STE2, the basal level of expression is modulated in the same manner.

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