scholarly journals The Cell Surface Flocculin Flo11 Is Required for Pseudohyphae Formation and Invasion bySaccharomyces cerevisiae

1998 ◽  
Vol 9 (1) ◽  
pp. 161-171 ◽  
Author(s):  
Wan-Sheng Lo ◽  
Anne M. Dranginis
Keyword(s):  
Cell Wall ◽  
Cell Surface ◽  
Mating Type ◽  
Nitrogen Starvation ◽  
Rich Media ◽  
Primary Means ◽  
A Cell ◽  
Consensus Binding Sequence ◽  
Diploid Cells ◽  
Binding Sequence

Diploid yeast develop pseudohyphae in response to nitrogen starvation, while haploid yeast produce invasive filaments which penetrate the agar in rich medium. We have identified a gene,FLO11, that encodes a cell wall protein which is critically required for both invasion and pseudohyphae formation in response to nitrogen starvation. FLO11 encodes a cell surface flocculin with a structure similar to the class of yeast serine/threonine-rich GPI-anchored cell wall proteins. Cells of theSaccharomyces cerevisiae strain Σ1278b with deletions of FLO11 do not form pseudohyphae as diploids nor invade agar as haploids. In rich media, FLO11 is regulated by mating type; it is expressed in haploid cells but not in diploids. Upon transfer to nitrogen starvation media, however, FLO11transcripts accumulate in diploid cells, but not in haploids. Overexpression of FLO11 in diploid cells, which are otherwise not invasive, enables them to invade agar. Thus, the mating type repression of FLO11 in diploids grown in rich media suffices to explain the inability of these cells to invade. The promoter of FLO11 contains a consensus binding sequence for Ste12p and Tec1p, proteins known to cooperatively activate transcription of Ty1 elements and theTEC1 gene during development of pseudohyphae. Yeast with a deletion of STE12 does not expressFLO11 transcripts, indicating that STE12is required for FLO11 expression. These ste12-deletion strains also do not invade agar. However, the ability to invade can be restored by overexpressing FLO11. Activation ofFLO11 may thus be the primary means by which Ste12p and Tec1p cause invasive growth.

Mating type control in Saccharomyces cerevisiae: a frameshift mutation at the common DNA sequence, X, of the HML alpha locus

1984 ◽  
Vol 4 (1) ◽  
pp. 203-211
Author(s):  
K Tanaka ◽  
T Oshima ◽  
H Araki ◽  
S Harashima ◽  
Y Oshima
Keyword(s):  
Mating Type ◽  
Base Pair ◽  
Reading Frame ◽  
Base Pair Deletion ◽  
A Cell ◽  
Alpha Gene ◽  
The Common ◽  
Type Switch ◽  
Diploid Cells ◽  
Mat Locus

A mutation defective in the homothallic switching of mating type alleles, designated hml alpha-2, has previously been characterized. The mutation occurred in a cell having the HO MATa HML alpha HMRa genotype, and the mutant culture consisted of ca. 10% a mating type cells, 90% nonmater cells of haploid cell size, and 0.1% sporogenous diploid cells. Genetic analyses revealed that nonmater haploid cells have a defect in the alpha 2 cistron at the MAT locus. This defect was probably caused by transposition of a cassette originating from the hml alpha-2 allele by the process of the homothallic mating type switch. That the MAT locus of the nonmater cells is occupied by a DNA fragment indistinguishable from the Y alpha sequence in electrophoretic mobility was demonstrated by Southern hybridization of the EcoRI-HindIII fragment encoding the MAT locus with a cloned HML alpha gene as the probe. The hml alpha-2 mutation was revealed to be a one-base-pair deletion at the ninth base pair in the X region from the X and Y boundary of the HML locus. This mutation gave rise to a shift in the open reading frame of the alpha 2 cistron. A molecular mechanism for the mating type switch associated with the occurrence of sporogenous diploid cells in the mutant culture is discussed.

scholarly journals The AWA1 Gene Is Required for the Foam-Forming Phenotype and Cell Surface Hydrophobicity of Sake Yeast

2002 ◽  
Vol 68 (4) ◽  
pp. 2018-2025 ◽  
Author(s):  
Hitoshi Shimoi ◽  
Kazutoshi Sakamoto ◽  
Masaki Okuda ◽  
Ratchanee Atthi ◽  
Kazuhiro Iwashita ◽  
...  
Keyword(s):  
Cell Wall ◽  
Cell Surface ◽  
Repetitive Sequences ◽  
Alcoholic Beverage ◽  
Cell Surface Hydrophobicity ◽  
Surface Hydrophobicity ◽  
A Cell ◽  
Characteristic Sequences ◽  
Foam Forming ◽  
Almost All

ABSTRACT Sake, a traditional alcoholic beverage in Japan, is brewed with sake yeasts, which are classified as Saccharomyces cerevisiae. Almost all sake yeasts form a thick foam layer on sake mash during the fermentation process because of their cell surface hydrophobicity, which increases the cells' affinity for bubbles. To reduce the amount of foam, nonfoaming mutants were bred from foaming sake yeasts. Nonfoaming mutants have hydrophilic cell surfaces and no affinity for bubbles. We have cloned a gene from a foam-forming sake yeast that confers foaming ability to a nonfoaming mutant. This gene was named AWA1 and structures of the gene and its product were analyzed. The N- and C-terminal regions of Awa1p have the characteristic sequences of a glycosylphosphatidylinositol anchor protein. The entire protein is rich in serine and threonine residues and has a lot of repetitive sequences. These results suggest that Awa1p is localized in the cell wall. This was confirmed by immunofluorescence microscopy and Western blotting analysis using hemagglutinin-tagged Awa1p. Moreover, an awa1 disruptant of sake yeast was hydrophilic and showed a nonfoaming phenotype in sake mash. We conclude that Awa1p is a cell wall protein and is required for the foam-forming phenotype and the cell surface hydrophobicity of sake yeast.

scholarly journals Flagellar adhesion in chlamydomonas induces synthesis of two high molecular weight cell surface proteins

1983 ◽  
Vol 96 (3) ◽  
pp. 589-597 ◽  
Author(s):  
WJ Snell ◽  
A Clausell ◽  
WS Moore
Keyword(s):  
Cell Wall ◽  
Cell Surface ◽  
Adhesion Molecules ◽  
Mating Type ◽  
Surface Proteins ◽  
Cell Wall Proteins ◽  
Intact Cells ◽  
Mating Reaction ◽  
Ionic Detergent ◽  
Flagellar Proteins

Because our previous studies (Snell, W.J., and W.S. Moore, 1980, J. Cell Biol. 84:203- 210) on the mating reaction of chlamydomonas reinhardtii showed that there was an adhesion-induced turnover of proteins whose synthesis is induced during aggregation. Analysis by SDS PAGE and autoradiography showed that proteins of 220,000 M(r) and 165, 000 M(r) (designated A(1) and A(2) respectively) consistently showed a high rate of synthesis only in flagella or flagellar membrane-enriched fractions prepared from aggregating gametes. Since the two proteins were soluble in the non-ionic detergent NP-40 and were removed from intact cells by a brief pronase treatment, it is likely that A(1) and A(2) are membrane proteins expose on the cell surface. A(1) and A(2) were each synthesized by gametes of both mating types (mt(-) and mt(+)) and synthesis of these two proteins could be detected in the normal mating reaction (wild type mt(-) and mt(+)), in mixtures of mt(-) and impotent mt(+) gametes (which could aggregate but not fuse), and in mixtures of gametes of a single mating type with isolated flagella of the opposite mating type. Cells aggregating in tunicamycin, an inhibitor of protein glycosylation, lost their adhesiveness during aggregation and did not synthesize the 220,000 M(r) protein but instead produced a protein (possibly an underglycosylated form of A(1)) of slightly lower mol wt. The 220,000 and 165,000 M(R) proteins appeared to be flagellar proteins and not cell wall proteins because A(1) and A(2) did not co-migrate with previously identified cell wall proteins, and synthesis of the two proteins could not be detected in flagella-less (bald-2) mutant cells. Analysis of the adhesive activity of sucrose gradient fraction of detergent (octyl glucoside)-solubilized flagellar membranes revealed that fractions containing A(1) and A(2) did not have detectable adhesive activity. The possibility remains that A(1) and A(2) are adhesion molecules whose activity could not be measured in the assay we used. Alternatively, the 220,000 and 165,000 M(r) proteins may be inactivated adhesion molecules or else they may be flagellar surface proteins involved only indirectly in the adhesion process.

Cell surface specific immunoglobulin inhibits α factor mediated morphogenesis in Saccharomyces cerevisiae

1987 ◽  
Vol 33 (4) ◽  
pp. 331-335
Author(s):  
Glenn J. Merkel ◽  
Charles L. Phelps ◽  
Roger W. Roeske
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Surface ◽  
Mating Type ◽  
Cell Envelope ◽  
Whole Cells ◽  
Cycle Arrest ◽  
Immunoglobulin Preparations ◽  
Specific Immunoglobulin ◽  
A Cell ◽  
Immunoglobulin Binding

Immunoglobulins raised from Saccharomyces cerevisiae a and α mating type cell envelope preparations inhibited α factor mediated morphogenesis of the a cell without inhibiting normal cell division. The Ig responsible for this inhibition was absorbed to both a and α whole cells and heat-killed cells, indicating that the immunoglobulin binding sites were exposed on the cell surface and not mating type specific. Additionally, α factor mediated cell cycle arrest was not affected by the immunoglobulin preparations, implying that the immunoglobulin was not preventing α factor from binding to its receptor.

scholarly journals A pathway for cell wall anchorage of Saccharomyces cerevisiae alpha-agglutinin.

1994 ◽  
Vol 14 (7) ◽  
pp. 4825-4833 ◽  
Author(s):  
C F Lu ◽  
J Kurjan ◽  
P N Lipke
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Plasma Membrane ◽  
Cell Surface ◽  
Soluble Form ◽  
Gpi Anchor ◽  
Glycosyl Phosphatidylinositol ◽  
Experimental Support ◽  
Cell Biol ◽  
A Cell

Saccharomyces cerevisiae alpha-agglutinin is a cell wall-anchored adhesion glycoprotein. The previously identified 140-kDa form, which contains a glycosyl-phosphatidylinositol (GPI) anchor (D. Wojciechowicz, C.-F. Lu, J. Kurjan, and P. N. Lipke, Mol. Cell. Biol. 13:2554-2563, 1993), and additional forms of 80, 150, 250 to 300, and > 300 kDa had the properties of intermediates in a transport and cell wall anchorage pathway. N glycosylation and additional modifications resulted in successive increases in size during transport. The 150- and 250- to 300-kDa forms were membrane associated and are likely to be intermediates between the 140-kDa form and a cell surface GPI-anchored form of > 300 kDa. A soluble form of > 300 kDa that lacked the GPI anchor had properties of a periplasmic intermediate between the plasma membrane form and the > 300-kDa cell wall-anchored form. These results constitute experimental support for the hypothesis that GPI anchors act to localize alpha-agglutinin to the plasma membrane and that cell wall anchorage involves release from the GPI anchor to produce a periplasmic intermediate followed by linkage to the cell wall.

scholarly journals Localized secretion of acid phosphatase reflects the pattern of cell surface growth in saccharomyces cerevisiae

1980 ◽  
Vol 86 (1) ◽  
pp. 123-128 ◽  
Author(s):  
C Field ◽  
R Schekman
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Acid Phosphatase ◽  
Cell Surface ◽  
Mating Type ◽  
Surface Growth ◽  
Parent Cell ◽  
Limited Growth ◽  
Yeast Cell Surface ◽  
Dividing Cells ◽  
A Cell

Secretion of cell wall-bound acid phosphatase by Saccharomyces cerevisiae occurs along a restricted portion of the cell surface. Acid phosphatase activity produced during derepressed synthesis on a phosphate-limited growth medium is detected with an enzyme-specific stain and is localized initially to the bud portion of a dividing cell. After two to three generations of phosphate-limited growth, most of the cells can be stained; if further phosphatase synthesis is repressed by growth in excess phosphate, dividing cells are produced in which the parent but not the bud can be stained. Budding growth is interrupted in α-mating-type cells by a pheromone (α-factor) secreted by the opposite mating type; cell surface growth continues in the presence of α-factor and produces a characteristic cell tip. When acid phosphatase synthesis is initiated during α-factor treatment, only the cell tip can br stained; when phosphate synthesis is repressed during α-factor treatment, the cell body but not the tip can be stained. A mixture of derepressed α cells and phosphatase-negative α cells form zygotes in which mainly one parent cell surface can be stained. The cell cycle mutant, cdc 24 (Hartwell, L.H. 1971. Exp. Cell Res. 69:265-276), fails to bud and, instead, expands symmetrically as a sphere at a nonpermissive temperature (37 degrees C). This mutant does not form a cell tip during α-factor treatment at 37 degrees C, and although acid phosphatade secretion occurs at this temperature, it is not localized. These results suggest that secretion reflects a polar mode of yeast cell- surface growth, and that this organization requires the cdc 24 gene product.

Structural Characterization of the Cell Wall Binding Domains of Clostridium difficile Toxins A and B; Evidence that Ca2+ Plays a Role in Toxin A Cell Surface Association

2005 ◽  
Vol 346 (5) ◽  
pp. 1197-1206 ◽  
Author(s):  
Stephen J. Demarest ◽  
Jared Salbato ◽  
Marikka Elia ◽  
Jingping Zhong ◽  
Theresa Morrow ◽  
...  
Keyword(s):  
Cell Wall ◽  
Clostridium Difficile ◽  
Cell Surface ◽  
Structural Characterization ◽  
Toxin A ◽  
Binding Domains ◽  
Cell Wall Binding ◽  
A Cell

A cell wall‐associated polysaccharide is required for bacteriophage adsorption to the Streptococcus thermophilus cell surface

2020 ◽  
Vol 114 (1) ◽  
pp. 31-45 ◽  
Author(s):  
Brian McDonnell ◽  
Laurens Hanemaaijer ◽  
Francesca Bottacini ◽  
Philip Kelleher ◽  
Katherine Lavelle ◽  
...  
Keyword(s):  
Cell Wall ◽  
Cell Surface ◽  
Streptococcus Thermophilus ◽  
A Cell

scholarly journals Mating type control in Saccharomyces cerevisiae: a frameshift mutation at the common DNA sequence, X, of the HML alpha locus.

1984 ◽  
Vol 4 (1) ◽  
pp. 203-211 ◽  
Author(s):  
K Tanaka ◽  
T Oshima ◽  
H Araki ◽  
S Harashima ◽  
Y Oshima
Keyword(s):  
Mating Type ◽  
Base Pair ◽  
Reading Frame ◽  
Base Pair Deletion ◽  
A Cell ◽  
Alpha Gene ◽  
The Common ◽  
Type Switch ◽  
Diploid Cells ◽  
Mat Locus

A mutation defective in the homothallic switching of mating type alleles, designated hml alpha-2, has previously been characterized. The mutation occurred in a cell having the HO MATa HML alpha HMRa genotype, and the mutant culture consisted of ca. 10% a mating type cells, 90% nonmater cells of haploid cell size, and 0.1% sporogenous diploid cells. Genetic analyses revealed that nonmater haploid cells have a defect in the alpha 2 cistron at the MAT locus. This defect was probably caused by transposition of a cassette originating from the hml alpha-2 allele by the process of the homothallic mating type switch. That the MAT locus of the nonmater cells is occupied by a DNA fragment indistinguishable from the Y alpha sequence in electrophoretic mobility was demonstrated by Southern hybridization of the EcoRI-HindIII fragment encoding the MAT locus with a cloned HML alpha gene as the probe. The hml alpha-2 mutation was revealed to be a one-base-pair deletion at the ninth base pair in the X region from the X and Y boundary of the HML locus. This mutation gave rise to a shift in the open reading frame of the alpha 2 cistron. A molecular mechanism for the mating type switch associated with the occurrence of sporogenous diploid cells in the mutant culture is discussed.

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