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 Genetic Characterization of a Cell Envelope-Associated Proteinase from Lactobacillus helveticus CNRZ32

1999 ◽  
Vol 181 (15) ◽  
pp. 4592-4597 ◽  
Author(s):  
Jeffrey A. Pederson ◽  
Gerald J. Mileski ◽  
Bart C. Weimer ◽  
James L. Steele
Keyword(s):  
Cell Surface ◽  
Deletion Mutant ◽  
Cell Envelope ◽  
Physiological Role ◽  
Lactobacillus Helveticus ◽  
Whole Cells ◽  
A Cell ◽  
Hydrolysis Of

ABSTRACT A cell envelope-associated proteinase gene (prtH) was identified in Lactobacillus helveticus CNRZ32. TheprtH gene encodes a protein of 1,849 amino acids and with a predicted molecular mass of 204 kDa. The deduced amino acid sequence of the prtH product has significant identity (45%) to that of the lactococcal PrtP proteinases. Southern blot analysis indicates thatprtH is not broadly distributed within L. helveticus. A prtH deletion mutant of CNRZ32 was constructed to evaluate the physiological role of PrtH. PrtH is not required for rapid growth or fast acid production in milk by CNRZ32. Cell surface proteinase activity and specificity were determined by hydrolysis of αs1-casein fragment 1-23 by whole cells. A comparison of CNRZ32 and its prtH deletion mutant indicates that CNRZ32 has at least two cell surface proteinases that differ in substrate specificity.

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.

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

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.

scholarly journals The use of flow microfluorimetry in the analysis of the phenotype expression of mouse histocompatibility antigens

1975 ◽  
Vol 64 (3) ◽  
pp. 719-724 ◽  
Author(s):  
GL Campbell ◽  
LT Goldstein ◽  
BB Knowles
Keyword(s):  
Cell Surface ◽  
Viable Cell ◽  
Cell Types ◽  
Parental Cell ◽  
Sample Population ◽  
Cell Surface Antigens ◽  
A Cell ◽  
Immunoglobulin Binding ◽  
Hybrid Clones ◽  
Lymphocyte Populations

Quantitation of the expression of cell surface antigens has hitherto been limited to analysis by either cytotoxicity tests or radioimmune assays (5, 15). We report here the use of a new methodology to analyze and quantitate the expression of mouse histocompabililty antigens (H-2 locus) in hybrid clones and parental cell types. The binding of fluorescein-tagged antibody is measured on a cell-to-cell basis in large viable cell populations using flow microfluorimetric techniques. These techniques have been used to measure hapten and immunoglobulin binding to lymphocyte populations (8, 9, 14). However, this is the first report in which these techniques have been used to examine the expression of the H-2 locus. The advantage of this approach is twofold: first, a large and statistically significant sample population may be analyzed one cell at a time, thus revealing the fine detail of heterogeneity in the expression of the cell surface markers within a population. Second, as has been demonstrated for analysis of specific components of the immune system, this method does permit fluorescence-activated sorting of cell types according to their different surface populations (8, 9, 14).

Cell cycle arrest and cellular differentiation mediated by a cell surface sialoglycopeptide

Life Sciences ◽  
1991 ◽  
Vol 48 (19) ◽  
pp. 1813-1820 ◽  
Author(s):  
Gregory D. Edson ◽  
Heideh K. Fattaey ◽  
Terry C. Johnson
Keyword(s):  
Cell Cycle ◽  
Cell Surface ◽  
Cell Cycle Arrest ◽  
Cellular Differentiation ◽  
Cycle Arrest ◽  
A Cell

Localization of the dicarboxylate binding protein in the cell envelope of Escherichia coli K12

1980 ◽  
Vol 58 (10) ◽  
pp. 885-897 ◽  
Author(s):  
Mary A. Bewick ◽  
Theodore C. Y. Lo
Keyword(s):  
Escherichia Coli ◽  
Cell Surface ◽  
Cell Envelope ◽  
Binding Protein ◽  
Osmotic Shock ◽  
Outer Region ◽  
Periplasmic Space ◽  
Whole Cells ◽  
Escherichia Coli K12 ◽  
The Moment

Examination of the localization of the dicarboxylate binding protein (DBP) in the cell envelope of Escherichia coli K12 reveals that this protein is present on the cell surface, and also in the inner and outer regions of the periplasmic space. The cell surface DBP is released by treating the cells with EDTA. This protein can be surface labeled by lactoperoxidase radio-iodination, and by diazo[125I]iodosulfanilic acid in whole cells. It also binds tightly, but not covalently, to lipopolysaccharide. The DBP located in the outer region of the periplasmic space is released when the outer membrane is dissociated by EDTA – osmotic shock treatment. The DBP located in the inner region of the periplasmic space is released only when the EDTA – osmotic shocked cells are subjected to lysozyme treatment. At the moment, it is not certain whether this protein is bound to or trapped by the peptidoglycan network. This protein cannot be surface labeled in whole cells or in EDTA – osmotic shock treated cells; and it is not associated with lipopolysaccharide. Analysis of transport mutants indicates that these DBP are coded by the same gene.

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

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.

scholarly journals LncRNAs of Saccharomyces cerevisiae dodge the cell cycle arrest imposed by the ethanol stress

2021 ◽  
Author(s):  
Lucas Cardoso Lázari ◽  
Ivan Rodrigo Wolf ◽  
Amanda Piveta Schnepper ◽  
Guilherme Targino Valente
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Cycle ◽  
Cell Cycle Arrest ◽  
Ethanol Stress ◽  
Network Dynamic ◽  
Cell Cycle Proteins ◽  
Tolerant Strain ◽  
Cycle Arrest ◽  
A Cell ◽  
The One

Ethanol impairs many subsystems of Saccharomyces cerevisiae, including the cell cycle. Cyclins and damage checkpoints drive the cell cycle. Two ethanol-responsive lncRNAs in yeast interact with cell cycle proteins, and here we investigated the role of these RNAs on the ethanol-stressed cell cycle. Our network dynamic modeling showed that the higher and lower ethanol tolerant strains undergo a cell cycle arrest during the ethanol stress. However, lower tolerant phenotype arrest in a later phase leading to its faster population rebound after the stress relief. Two lncRNAs can skip the arrests mentioned. The in silico overexpression of lnc9136 of SEY6210 (a lower tolerant strain), and CRISPR-Cas9 partial deletions of this lncRNA, evidenced that the one induces a regular cell cycle even under ethanol stress; this lncRNA binds to Gin4 and Hsl1, driving the Swe1p, Clb1/2, and cell cycle. Moreover, the lnc10883 of BY4742 (a higher tolerant strain) interacts to the Mec1p and represses Bub1p, circumventing the DNA and spindle damage checkpoints keeping a normal cell cycle even under DNA damage. Overall, we present the first evidence of the direct roles of lncRNAs on cell cycle proteins, the dynamics of this system in different ethanol tolerant phenotypes, and a new cell cycle model.

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