scholarly journals Adenylyl cyclase is dispensable for vegetative cell growth in the fission yeast Schizosaccharomyces pombe.

1990 ◽  
Vol 87 (20) ◽  
pp. 7814-7818 ◽  
Author(s):  
T. Maeda ◽  
N. Mochizuki ◽  
M. Yamamoto
Keyword(s):  
Cell Growth ◽  
Schizosaccharomyces Pombe ◽  
Adenylyl Cyclase ◽  
Fission Yeast ◽  
Vegetative Cell

scholarly journals Phosphatidylethanolamine Is Required for Normal Cell Morphology and Cytokinesis in the Fission Yeast Schizosaccharomyces pombe

2009 ◽  
Vol 8 (5) ◽  
pp. 790-799 ◽  
Author(s):  
Jun Luo ◽  
Yasuhiro Matsuo ◽  
Galina Gulis ◽  
Haylee Hinz ◽  
Jana Patton-Vogt ◽  
...  
Keyword(s):  
Cell Growth ◽  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Minimal Medium ◽  
Growth Media ◽  
Decarboxylase Activity ◽  
Rich Medium ◽  
Wild Type ◽  
Cellular Functions ◽  
Kennedy Pathway

ABSTRACT To investigate the contributions of phosphatidylethanolamine to the growth and morphogenesis of the fission yeast Schizosaccharomyces pombe, we have characterized three predicted genes in this organism, designated psd1, psd2, and psd3, encoding phosphatidylserine decarboxylases, which catalyze the conversion of phosphatidylserine to phosphatidylethanolamine in both eukaryotic and prokaryotic organisms. S. pombe mutants carrying deletions in any one or two psd genes are viable in complex rich medium and synthetic defined minimal medium. However, mutants carrying deletions in all three psd genes (psd1-3Δ mutants) grow slowly in rich medium and are inviable in minimal medium, indicating that the psd1 to psd3 gene products share overlapping essential cellular functions. Supplementation of growth media with ethanolamine, which can be converted to phosphatidylethanolamine by the Kennedy pathway, restores growth to psd1-3Δ cells in minimal medium, indicating that phosphatidylethanolamine is essential for S. pombe cell growth. psd1-3Δ cells produce lower levels of phosphatidylethanolamine than wild-type cells, even in medium supplemented with ethanolamine, indicating that the Kennedy pathway can only partially compensate for the loss of phosphatidylserine decarboxylase activity in S. pombe. psd1-3Δ cells appear morphologically indistinguishable from wild-type S. pombe cells in medium supplemented with ethanolamine, but when cultured in nonsupplemented medium, they produce high frequencies of abnormally shaped cells as well as cells exhibiting severe septation defects, including multiple, mispositioned, deformed, and misoriented septa. Our results demonstrate that phosphatidylethanolamine is essential for cell growth and for normal cytokinesis and cellular morphogenesis in S. pombe, and they illustrate the usefulness of this model eukaryote for investigating potentially conserved biological and molecular functions of phosphatidylethanolamine.

scholarly journals The concerted actions of Tip1/CLIP-170, Klp5/Kinesin-8, and Alp14/XMAP215 regulate microtubule catastrophe at the cell end

2019 ◽  
Vol 11 (11) ◽  
pp. 956-966 ◽  
Author(s):  
Xiaojia Niu ◽  
Fan Zheng ◽  
Chuanhai Fu
Keyword(s):  
Cell Growth ◽  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Cell Polarity ◽  
Residence Time ◽  
Dependent Manner ◽  
Spatial Regulation ◽  
Live Cell Microscopy ◽  
Stabilizing Factors ◽  
Cell Microscopy

Abstract Spatial regulation of microtubule catastrophe is important for controlling microtubule length and consequently contributes to the proper establishment of cell polarity and cell growth. The +TIP proteins including Tip1/CLIP-170, Klp5/Kinesin-8, and Alp14/XMAP215 reside at microtubule plus ends to regulate microtubule dynamics. In the fission yeast Schizosaccharomyces pombe, Tip1 and Alp14 serve as microtubule-stabilizing factors, while Klp5 functions oppositely as a catastrophe-promoting factor. Despite that Tip1 has been shown to play a key role in restricting microtubule catastrophe to the cell end, how Tip1 fulfills the role remains to be determined. Employing live-cell microscopy, we showed that the absence of Tip1 impairs the localization of both Klp5 and Alp14 at microtubule plus ends, but the absence of Klp5 prolongs the residence time of Tip1 at microtubule plus ends. We further revealed that Klp5 accumulates behind Tip1 at microtubule plus ends in a Tip1-dependent manner. In addition, artificially tethering Klp5 to microtubule plus ends promotes premature microtubule catastrophe, while tethering Alp14 to microtubule plus ends in the cells lacking Tip1 rescues the phenotype of short microtubules. These findings establish that Tip1 restricts microtubule catastrophe to the cell end likely by spatially restricting the microtubule catastrophe activity of Klp5 and stabilizing Alp14 at microtubule plus ends. Thus, the work demonstrates the orchestration of Tip1, Alp14, and Klp5 in ensuring microtubule catastrophe at the cell end.

scholarly journals Adenylyl cyclase activity of the fission yeast Schizosaccharomyces pombe is not regulated by guanyl nucleotides

FEBS Letters ◽  
1990 ◽  
Vol 261 (2) ◽  
pp. 413-418 ◽  
Author(s):  
David Engelberg ◽  
Enrique Poradosu ◽  
Giora Simchen ◽  
Alexander Levitzki
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Adenylyl Cyclase ◽  
Fission Yeast ◽  
Cyclase Activity ◽  
Adenylyl Cyclase Activity

Calmodulin localizes to the spindle pole body of Schizosaccharomyces pombe and performs an essential function in chromosome segregation

1997 ◽  
Vol 110 (15) ◽  
pp. 1805-1812 ◽  
Author(s):  
M.J. Moser ◽  
M.R. Flory ◽  
T.N. Davis
Keyword(s):  
Cell Growth ◽  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Chromosome Segregation ◽  
Fluorescent Protein ◽  
Budding Yeast ◽  
Spindle Pole Body ◽  
Spindle Pole ◽  
Temperature Sensitive ◽  
Pole Body

The essential calmodulin genes in both Saccharomyces cerevisiae and Schizosaccharomyces pombe were precisely replaced with genes encoding fusions between calmodulin and the green fluorescent protein (GFP). In living budding yeast the GFP-calmodulin fusion protein (GFP-Cmd1p) localized simultaneously to sites of cell growth and to the spindle pole body (SPB), the yeast analog of the centrosome. Having demonstrated proper localization of GFP-calmodulin in budding yeast, we examined the localization of a fusion between GFP and calmodulin (GFP-Camlp) in fission yeast, where calmodulin had not been localized by any method. We find GFP-Camlp also localizes both to sites of polarized cell growth and to the fission yeast SPB. The localization of calmodulin to the SPB by GFP fusion was confirmed by indirect immunofluorescence. Antiserum to S. pombe calmodulin labeled the ends of the mitotic spindle stained with anti-tubulin antiserum. This pattern was identical to that seen using antiserum to Sad1p, a known SPB component. We then characterized the defects in a temperature-sensitive S. pombe calmodulin mutant. Mutant cam1-E14 cells synchronized in S phase completed DNA synthesis, but lost viability during transit of mitosis. Severe defects in chromosome segregation, including hypercondensation, fragmentation, and unequal allocation of chromosomal material were observed. Immunofluorescence analysis of tubulin revealed a population of cells containing either broken or mislocalized mitotic spindles, which were never observed in wild-type cells. Taken together with the subcellular localization of calmodulin, the observed spindle and chromosome segregation defects suggest that calmodulin performs an essential role during mitosis at the fission yeast SPB.

scholarly journals Isolation of protein glycosylation mutants in the fission yeast Schizosaccharomyces pombe.

1995 ◽  
Vol 6 (5) ◽  
pp. 485-496 ◽  
Author(s):  
K M Huang ◽  
M D Snider
Keyword(s):  
Cell Wall ◽  
Acid Phosphatase ◽  
Cell Growth ◽  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Electrophoretic Mobility ◽  
Protein Glycosylation ◽  
Wild Type ◽  
Glycoprotein Synthesis ◽  
Lectin Staining

We have isolated mutants in the fission yeast Schizosaccharomyces pombe that are defective in protein glycosylation. A collection of osmotically sensitive mutants was prepared and screened for glycosylation defects using lectin staining as an assay. Mutants singly defective in four glycoprotein synthesis genes (gps1-4) were isolated, all of which bind less galactose-specific lectin. Acid phosphatase and other glycoproteins from the gps mutants have increased electrophoretic mobility, suggesting that these mutants make glycans of reduced size. N-linked glycan analysis revealed that terminal oligosaccharide modification is defective in the gps1 and gps2 mutants. Both mutants synthesize the Man9GlcNAc2 core glycan but have reduced amounts of larger structures. Modified core glycans from gps1 cells have normal amounts of galactose (Gal) residues, but reduced amounts of Man, consistent with a defect in a Golgi mannosyltransferase in this mutant. In contrast, N-linked oligosaccharides from gps2 mutants have much less Gal than wild type, because of reduced levels of the Gal donor, UDP-Gal. This reduction is caused by decreased activity of UDP-glucose 4-epimerase, which synthesizes UDP-Gal. Neither the gps1 or gps2 mutations are lethal, although the cells grow at reduced rates. These findings suggest that S. pombe cells can survive with incompletely glycosylated cell wall glycoproteins. In particular, these results suggest that Gal, which comprises approximately 30% by weight of cell wall glycoprotein glycans, is not crucial for cell growth or survival.

Ascorbic acid supplementation suppresses cadmium-derived alterations in the fission yeast Schizosaccharomyces pombe

10.5219/1618 ◽  
2021 ◽  
Vol 15 ◽  
pp. 423-432
Author(s):  
Marek Kovár ◽  
Alica Navrátilová ◽  
Anna Trakovická ◽  
Miroslava Požgajová
Keyword(s):  
Ascorbic Acid ◽  
Cell Growth ◽  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Membrane Lipids ◽  
Cadmium Toxicity ◽  
Model Organism ◽  
Cell Types ◽  
Dependent Manner ◽  
The Impact

Cadmium (Cd) a highly toxic environmental pollutant, that does not have any physiological function in the organism, represents a great concern for human health as it can be easily transported from its environmental sources to the food chain. Food, water, and air are the major sources of Cd exposure to the population. Cd-mediated impairments of the basic cellular properties largely depend on its ability to enhance the formation of reactive oxygen species (ROS) and thus triggers oxidative stress to the cell. With the use of fission yeast Schizosaccharomyces pombe (S. pombe) as the model organism, we have analyzed the impact of Cd on the cell growth intensity, as it represents the fundamental feature of all living organisms. Cells were incubated with different Cd concentrations for 3, 6, and 9 hours to investigate the effect of Cd on cell growth in a time and dose-dependent manner. Further possible Cd-derived alterations, as the peroxidation of membrane lipids or the functional impairment of the enzymatic antioxidant protection mechanisms, were investigated by determination of the MDA content and via catalase (CAT) activity detection. Moreover, ascorbic acid (AsA) pre-treatment was subjected to investigate the assumed positive effect of AsA against Cd toxicity. We show here on one hand that cells suffer under the influence of Cd, but on the other hand, they substantially profit from AsA supplementation. Because S. pombe is known to shares many molecular, and biochemical similarities with higher organisms, the effect of AsA in cadmium toxicity elimination might be expected to a similar extent also in other cell types.

Use of PKA-mediated phenotypes for genetic and small-molecule screens in Schizosaccharomyces pombe

2013 ◽  
Vol 41 (6) ◽  
pp. 1692-1695 ◽  
Author(s):  
Ana Santos de Medeiros ◽  
Alexander Magee ◽  
Kyle Nelson ◽  
Liora Friedberg ◽  
Karolina Trocka ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Cell Growth ◽  
Schizosaccharomyces Pombe ◽  
Protein Kinase A ◽  
Fission Yeast ◽  
Small Molecule ◽  
Sexual Development ◽  
Cyclic Nucleotide ◽  
Pka Pathway ◽  
Kinase A

PKA (protein kinase A) in the fission yeast Schizosaccharomyces pombe controls transcription of genes involved in metabolism, cell growth and sexual development. In the present review, we discuss phenotypes associated with either high or low PKA activity in the context of how they can be used to carry out genetic or small-molecule screens that affect components of the PKA pathway. Although our recent research has focused on the study of heterologously expressed cyclic nucleotide PDEs (phosphodiesterases), these same methods can be used to target other S. pombe proteins or their functionally equivalent orthologues that act in the PKA pathway.

Overexpression of a metacaspase gene stimulates cell growth and stress response inSchizosaccharomyces pombe

2007 ◽  
Vol 53 (8) ◽  
pp. 1016-1023 ◽  
Author(s):  
Hye-Won Lim ◽  
Su-Jung Kim ◽  
Eun-Hee Park ◽  
Chang-Jin Lim
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Stress Response ◽  
Cell Growth ◽  
Schizosaccharomyces Pombe ◽  
Sodium Nitroprusside ◽  
Fission Yeast ◽  
Recombinant Plasmid ◽  
Mrna Level ◽  
Yeast Cells ◽  
Yeast Saccharomyces Cerevisiae

A unique gene named pca1+, encoding a metacaspase, was cloned from the fission yeast Schizosaccharomyces pombe and was used to create a recombinant plasmid, pPMC. The metacaspase mRNA level was markedly elevated in the fission yeast cells harboring the plasmid pPMC. Overexpressed Pca1+appeared to stimulate the growth of the fission yeast cells instead of arresting their growth. Its expression was enhanced by stress-inducing agents such as H2O2, sodium nitroprusside, and CdCl2, and it conferred cytoprotection, especially against CdCl2. However, such protection was not reproducible in the budding yeast Saccharomyces cerevisiae harboring pPMC. Taken together, these results propose that Pca1+may be involved in the growth and stress response of the fission yeast.

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