scholarly journals Solubilization and characterization of a cell wall-bound trehalase from ascospores of the fission yeast Schizosaccharomyces pombe

2009 ◽  
Vol 164 (3) ◽  
pp. 304-311 ◽  
Author(s):  
J. Vicente-Soler ◽  
T. Soto ◽  
M. Madrid ◽  
A. Núñez ◽  
J. Cansado ◽  
...  
Keyword(s):  
Cell Wall ◽  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
A Cell

scholarly journals Novel Rho GTPase Involved in Cytokinesis and Cell Wall Integrity in the Fission Yeast Schizosaccharomyces pombe

2003 ◽  
Vol 2 (3) ◽  
pp. 521-533 ◽  
Author(s):  
Beatriz Santos ◽  
Javier Gutiérrez ◽  
Teresa M. Calonge ◽  
Pilar Pérez
Keyword(s):  
Cell Wall ◽  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Rho Gtpases ◽  
Rho Gtpase ◽  
Cell Wall Integrity ◽  
Glucan Synthase ◽  
Actin Organization ◽  
Morphological Defects

ABSTRACT The Rho family of GTPases is present in all eukaryotic cells from yeast to mammals; they are regulators in signaling pathways that control actin organization and morphogenetic processes. In yeast, Rho GTPases are implicated in cell polarity processes and cell wall biosynthesis. It is known that Rho1 and Rho2 are key proteins in the construction of the cell wall, an essential structure that in Schizosaccharomyces pombe is composed of β-glucan, α-glucan, and mannoproteins. Rho1 regulates the synthesis of 1,3-β-d-glucan by activation of the 1,3-β-d-glucan synthase, and Rho2 regulates the synthesis of α-glucan by the 1,3-α-d-glucan synthase Mok1. Here we describe the characterization of another Rho GTPase in fission yeast, Rho4. rho4Δ cells are viable but display cell separation defects at high temperature. In agreement with this observation, Rho4 localizes to the septum. Overexpression of rho4 + causes lysis and morphological defects. Several lines of evidence indicate that both rho4 + deletion or rho4 + overexpression result in a defective cell wall, suggesting an additional role for Rho4 in cell wall integrity. rho4Δ cells also accumulate secretory vesicles around the septum and are defective in actin polarization. We propose that Rho4 could be involved in the regulation of the septum degradation during cytokinesis.

scholarly journals Characterization of Glycoside Hydrolase Family 5 Proteins in Schizosaccharomyces pombe

2010 ◽  
Vol 9 (11) ◽  
pp. 1650-1660 ◽  
Author(s):  
Encarnación Dueñas-Santero ◽  
Ana Belén Martín-Cuadrado ◽  
Thierry Fontaine ◽  
Jean-Paul Latgé ◽  
Francisco del Rey ◽  
...  
Keyword(s):  
Cell Wall ◽  
Schizosaccharomyces Pombe ◽  
Protein Characterization ◽  
Wall Material ◽  
Glycoside Hydrolase Family ◽  
Content Type ◽  
Hydrolysis Of ◽  
Controlled Hydrolysis ◽  
Hydrolase Family

ABSTRACT In yeast, enzymes with β-glucanase activity are thought to be necessary in morphogenetic events that require controlled hydrolysis of the cell wall. Comparison of the sequence of the Saccharomyces cerevisiae exo-β(1,3)-glucanase Exg1 with the Schizosaccharomyces pombe genome allowed the identification of three genes that were named exg1 + (locus SPBC1105.05), exg2 + (SPAC12B10.11), and exg3 + (SPBC2D10.05). The three proteins have different localizations: Exg1 is secreted to the periplasmic space, Exg2 is a membrane protein, and Exg3 is a cytoplasmic protein. Characterization of the biochemical activity of the proteins indicated that Exg1 and Exg3 are active only against β(1,6)-glucans while no activity was detected for Exg2. Interestingly, Exg1 cleaves the glucans with an endohydrolytic mode of action. exg1 + showed periodic expression during the cell cycle, with a maximum coinciding with the septation process, and its expression was dependent on the transcription factor Sep1. The Exg1 protein localizes to the septum region in a pattern that was different from that of the endo-β(1,3)-glucanase Eng1. Overexpression of Exg2 resulted in an increase in cell wall material at the poles and in the septum, but the putative catalytic activity of the protein was not required for this effect.

Isolation and first characterization of a cell-wall-degrading agent of Chlorella

1979 ◽  
Vol 66 (10) ◽  
pp. 525-526 ◽  
Author(s):  
G. Touet ◽  
H. G. Aach
Keyword(s):  
Cell Wall ◽  
A Cell

Analysis of the structural genes encoding M-factor in the fission yeast Schizosaccharomyces pombe: identification of a third gene, mfm3

1994 ◽  
Vol 14 (6) ◽  
pp. 3895-3905
Author(s):  
S Kjaerulff ◽  
J Davey ◽  
O Nielsen
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Mutational Analysis ◽  
M Cells ◽  
Gene Products ◽  
Structural Genes ◽  
Triple Mutant ◽  
Isolation And Characterization ◽  
Genes Encoding

We previously identified two genes, mfm1 and mfm2, with the potential to encode the M-factor mating pheromone of the fission yeast Schizosaccharomyces pombe (J. Davey, EMBO J. 11:951-960, 1992), but further analysis revealed that a mutant strain lacking both genes still produced active M-factor. Here we describe the isolation and characterization of a third M-factor gene, mfm3. A mutant lacking all three genes fails to produce M-factor, indicating that all functional M-factor genes now have been identified. The triple mutant exhibits an absolute mating defect in M cells, a defect that is not rescued by addition of exogenous M-factor. A mutational analysis reveals that all three mfm genes contribute to the production of M-factor. Their transcription is limited to M cells and requires the mat1-Mc and ste11 gene products. Each gene is induced when the cells are starved of nitrogen and further induced by a pheromone signal. Additionally, the signal transduction machinery associated with the pheromone response is required for transcription of the mfm genes in both stimulated and unstimulated cells.

scholarly journals Phylogenetic and comparative functional analysis of the cell-separation α-glucanase Agn1p in Schizosaccharomyces

Microbiology ◽  
2014 ◽  
Vol 160 (6) ◽  
pp. 1063-1074 ◽  
Author(s):  
Matthias Sipiczki ◽  
Anita Balazs ◽  
Aniko Monus ◽  
Laszlo Papp ◽  
Anna Horvath ◽  
...  
Keyword(s):  
Cell Wall ◽  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Mother Cell ◽  
Cell Separation ◽  
Yeast Cells ◽  
Glycoside Hydrolase Family ◽  
Binding Domains ◽  
Yeast Phase ◽  
Mother Cell Wall

The post-cytokinetic separation of cells in cell-walled organisms involves enzymic processes that degrade a specific layer of the division septum and the region of the mother cell wall that edges the septum. In the fission yeast Schizosaccharomyces pombe, the 1,3-α-glucanase Agn1p, originally identified as a mutanase-like glycoside hydrolase family 71 (GH71) enzyme, dissolves the mother cell wall around the septum edge. Our search in the genomes of completely sequenced fungi identified GH71 hydrolases in Basidiomycota, Taphrinomycotina and Pezizomycotina, but not in Saccharomycotina. The most likely Agn1p orthologues in Pezizomycotina species are not mutanases having mutanase-binding domains, but experimentally non-characterized hypothetical proteins that have no carbohydrate-binding domains. The analysis of the GH71 domains corroborated the phylogenetic relationships of the Schizosaccharomyces species determined by previous studies, but suggested a closer relationship to the Basidiomycota proteins than to the Ascomycota proteins. In the Schizosaccharomyces genus, the Agn1p proteins are structurally conserved: their GH71 domains are flanked by N-terminal secretion signals and C-terminal sequences containing the conserved block YNFNAY/HTG. The inactivation of the agn1Sj gene in Schizosaccharomyces japonicus, the only true dimorphic member of the genus, caused a severe cell-separation defect in its yeast phase, but had no effect on the hyphal growth and yeast-to-mycelium transition. It did not affect the mycelium-to-yeast transition either, only delaying the separation of the yeast cells arising from the fragmenting hyphae. The heterologous expression of agn1Sj partially rescued the separation defect of the agn1Δ cells of Schizosaccharomyces pombe. The results presented indicate that the fission yeast Agn1p 1,3-α-glucanases of Schizosaccharomyces japonicus and Schizosaccharomyces pombe share conserved functions in the yeast phase.

Sign in / Sign up

Export Citation Format

Share Document