Identification and characterization of a major building block in the cell wall of Saccharomyces cerevisiae

1997 ◽  
Vol 25 (3) ◽  
pp. 856-860 ◽  
Author(s):  
F. M. Klis ◽  
L. H. P. Caro ◽  
J. H. Vossen ◽  
J. C. Kapteyn ◽  
A. F. J. Ram ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Building Block ◽  
Identification And Characterization

IDENTIFICATION AND CHARACTERIZATION OF A MAJOR BUILDING BLOCK IN THE FUNGAL CELL WALL

1997 ◽  
Vol 25 (3) ◽  
pp. 419S-419S
Author(s):  
Frans M. Klis ◽  
L. Heleen P. Caro ◽  
Jack H. Vossen ◽  
M. Van Der Vaart ◽  
Herman Van Den Ende
Keyword(s):  
Cell Wall ◽  
Building Block ◽  
Fungal Cell Wall ◽  
Fungal Cell ◽  
Identification And Characterization

scholarly journals The Identification and Characterization of ADR6, a Gene Required for Sporulation and for Expression of the Alcohol Dehydrogenase II Isozyme From Saccharomyces cerevisiae

Genetics ◽  
1987 ◽  
Vol 116 (4) ◽  
pp. 523-530
Author(s):  
Aileen K W Taguchi ◽  
Elton T Young
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Alcohol Dehydrogenase ◽  
Isocitrate Lyase ◽  
Carbon Sources ◽  
Recessive Mutation ◽  
Yeast Saccharomyces Cerevisiae ◽  
Upstream Activating Sequence ◽  
Adh Activity ◽  
Identification And Characterization

ABSTRACT The alcohol dehydrogenase II isozyme (enzyme, ADHII; structural gene, ADH2) of the yeast, Saccharomyces cerevisiae, is under stringent carbon catabolite control. This cytoplasmic isozyme exhibits negligible activity during growth in media containing fermentable carbon sources such as glucose and is maximal during growth on nonfermentable carbon sources. A recessive mutation, adr6-1, and possibly two other alleles at this locus, were selected for their ability to decrease Ty-activated ADH2-6 c expression. The adr6-1 mutation led to decreased ADHII activity in both ADH2-6c and ADH2+ strains, and to decreased levels of ADH2 mRNA. Ty transcription and the expression of two other carbon catabolite regulated enzymes, isocitrate lyase and malate dehydrogenase, were unaffected by the adr6-1 mutation. adr6-1/adr6-1strains were defective for sporulation, indicating that adr6 mutations may have pleiotropic effects. The sporulation defect was not a consequence of decreased ADH activity. Since the ADH2-6c mutation is due to insertion of a 5.6-kb Ty element at the TATAA box, it appears that the ADR6+-dependent ADHII activity required ADH2 sequences 3′ to or including the TATAA box. The ADH2 upstream activating sequence (UAS) was probably not required. The ADR6 locus was unlinked to the ADR1 gene which encodes another trans-acting element required for ADH2 expression.

scholarly journals Characterization of Cell Wall Proteins in Saccharomyces cerevisiae Clinical Isolates Elucidates Hsp150p in Virulence

PLoS ONE ◽  
2015 ◽  
Vol 10 (8) ◽  
pp. e0135174 ◽  
Author(s):  
Pang-Hung Hsu ◽  
Pei-Chi Chiang ◽  
Chia-Hsun Liu ◽  
Ya-Wen Chang
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Clinical Isolates ◽  
Cell Wall Proteins

scholarly journals Calcofluor Antifungal Action Depends on Chitin and a Functional High-Osmolarity Glycerol Response (HOG) Pathway: Evidence for a Physiological Role of the Saccharomyces cerevisiae HOG Pathway under Noninducing Conditions

2000 ◽  
Vol 182 (9) ◽  
pp. 2428-2437 ◽  
Author(s):  
L. J. García-Rodriguez ◽  
A. Durán ◽  
C. Roncero
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Protein Kinase ◽  
Salt Tolerance ◽  
Map Kinases ◽  
Physiological Role ◽  
Hog Pathway ◽  
High Osmolarity ◽  
High Osmolarity Glycerol

ABSTRACT We have isolated several Saccharomyces cerevisiaemutants resistant to calcofluor that contain mutations in thePBS2 or HOG1 genes, which encode the mitogen-activated protein kinase (MAPK) and MAP kinases, respectively, of the high-osmolarity glycerol response (HOG) pathway. We report that blockage of either of the two activation branches of the pathway, namely, SHO1 and SLN1, leads to partial resistance to calcofluor, while simultaneous disruption significantly increases resistance. However, chitin biosynthesis is independent of the HOG pathway. Calcofluor treatment also induces an increase in salt tolerance and glycerol accumulation, although no activation of the HOG pathway is detected. Our results indicate that the antifungal effect of calcofluor depends on its binding to cell wall chitin but also on the presence of a functional HOG pathway. Characterization of one of the mutants isolated, pbs2-14, revealed that resistance to calcofluor and HOG-dependent osmoadaptation are two different physiological processes. Sensitivity to calcofluor depends on the constitutive functionality of the HOG pathway; when this is altered, the cells become calcofluor resistant but also show very low levels of basal salt tolerance. Characterization of some multicopy suppressors of the calcofluor resistance phenotype indicated that constitutive HOG functionality participates in the maintenance of cell wall architecture, a conclusion supported by the antagonism observed between the protein kinase and HOG signal transduction pathways.

Identification and characterization of four new GCD genes in Saccharomyces cerevisiae

1986 ◽  
Vol 10 (9) ◽  
pp. 657-664 ◽  
Author(s):  
Peter Niederberger ◽  
Markus Aebi ◽  
Ralf H�tter
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Identification And Characterization
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