scholarly journals Molecular cloning of a cell wall exo-beta-1,3-glucanase from Saccharomyces cerevisiae.

1989 ◽  
Vol 171 (11) ◽  
pp. 6259-6264 ◽  
Author(s):  
F Klebl ◽  
W Tanner
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Molecular Cloning ◽  
A Cell

scholarly journals Construction of a Library of Human Glycosyltransferases Immobilized in the Cell Wall of Saccharomyces cerevisiae

2006 ◽  
Vol 72 (11) ◽  
pp. 7003-7012 ◽  
Author(s):  
Yoh-ichi Shimma ◽  
Fumie Saito ◽  
Fumi Oosawa ◽  
Yoshifumi Jigami
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Yeast Cell ◽  
Protein Disulfide Isomerase ◽  
Immobilized Enzymes ◽  
Enzymatic Activities ◽  
Yeast Cell Wall ◽  
Yeast Protein ◽  
A Cell ◽  
Protein Disulfide

ABSTRACT Fifty-one human glycosyltransferases were expressed in Saccharomyces cerevisiae as immobilized enzymes and were assayed for enzymatic activities. The stem and catalytic regions of sialyl-, fucosyl-, galactosyl-, N-acetylgalactosaminyl-, and N-acetylglucosaminyltransferases were fused with yeast cell wall Pir proteins, which anchor glycosyltransferases at the yeast cell wall glucan. More than 75% of expressed recombinant glycosyltransferases retained their enzymatic activities in the yeast cell wall fraction and will be used as a human glycosyltransferase library. In increasing the enzymatic activities of immobilized glycosyltransferases, several approaches were found to be effective. Additional expression of yeast protein disulfide isomerase increased the expression levels and activities of polypeptide N-acetylgalactosaminyltransferases and other glycosyltransferases. PIR3 and/or PIR4 was more effective than PIR1 as a cell wall anchor when the Pir-glycosyltransferase fusions were expressed under the control of the constitutive glyceraldehyde-3-phosphate dehydrogenase promoter. Oligosaccharides such as Lewis x, Lewis y, and H antigen were successfully synthesized using this immobilized glycosyltransferase library, indicating that the Pir-fused glycosyltransferases are useful for the production of various human oligosaccharides.

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 Phylogenetic origin and transcriptional regulation at the post-diauxic phase of SPI1, in Saccharomyces cerevisiae

2012 ◽  
Vol 17 (3) ◽  
Author(s):  
Fernando Cardona ◽  
Marcel.Lí Olmo ◽  
Agustín Aranda
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Transcriptional Regulation ◽  
Stationary Phases ◽  
Cell Wall Protein ◽  
Null Mutant ◽  
Common Features ◽  
A Cell ◽  
Phylogenetic Origin ◽  
Pka Pathway

AbstractThe gene SPI1, of Saccharomyces cerevisiae, encodes a cell wall protein that is induced in several stress conditions, particularly in the postdiauxic and stationary phases of growth. It has a paralogue, SED1, which shows some common features in expression regulation and in the null mutant phenotype. In this work we have identified homologues in other species of yeasts and filamentous fungi, and we have also elucidated some aspects of the origin of SPI1, by duplication and diversification of SED1. In terms of regulation, we have found that the expression in the post-diauxic phase is regulated by genes related to the PKA pathway and stress response (MSN2/4, YAK1, POP2, SOK2, PHD1, and PHO84) and by genes involved in the PKC pathway (WSC2, PKC1, and MPK1).

Comparison of β-Glucan Structures in a Cell Wall Mutant of Saccharomyces cerevisiae and the Wild Type

1985 ◽  
Vol 98 (5) ◽  
pp. 1301-1307 ◽  
Author(s):  
Masao SHIOTA ◽  
Tasuku NAKAJIMA ◽  
Atsuko SATOH ◽  
Mariko SHIDA ◽  
Kazuo MATSUDA
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Wild Type ◽  
A Cell

scholarly journals Lack of GTP-bound Rho1p in secretory vesicles of Saccharomyces cerevisiae

2003 ◽  
Vol 162 (1) ◽  
pp. 85-97 ◽  
Author(s):  
Mitsuhiro Abe ◽  
Hiroshi Qadota ◽  
Aiko Hirata ◽  
Yoshikazu Ohya
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Plasma Membrane ◽  
Vesicular Transport ◽  
Secretory Vesicles ◽  
Glucan Synthase ◽  
Exchange Factor ◽  
Inactive Form ◽  
A Cell

Rho1p, an essential Rho-type GTPase in Saccharomyces cerevisiae, activates its effectors in the GTP-bound form. Here, we show that Rho1p in secretory vesicles cannot activate 1,3-β-glucan synthase, a cell wall synthesizing enzyme, during vesicular transport to the plasma membrane. Analyses with an antibody preferentially reacting with the GTP-bound form of Rho1p revealed that Rho1p remains in the inactive form in secretory vesicles. Rom2p, the GDP/GTP exchange factor of Rho1p, is preferentially localized on the plasma membrane even when vesicular transport is blocked. Overexpression of Rom2p results in delocalization of Rom2p and accumulation of 1,3-β-glucan in secretory vesicles. Based on these results, we propose that Rho1p is kept inactive in intracellular secretory organelles, resulting in repression of the activity of the cell wall–synthesizing enzyme within cells.

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 Binding of yeast killer toxin to a cell wall receptor on sensitive Saccharomyces cerevisiae.

1979 ◽  
Vol 140 (3) ◽  
pp. 888-892 ◽  
Author(s):  
H Bussey ◽  
D Saville ◽  
K Hutchins ◽  
R G Palfree
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Killer Toxin ◽  
A Cell ◽  
Yeast Killer ◽  
Yeast Killer Toxin
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