scholarly journals A homolog of mammalian antizyme is present in fission yeast Schizosaccharomyces pombe but not detected in budding yeast Saccharomyces cerevisiae

2000 ◽  
Vol 16 (5) ◽  
pp. 478-481 ◽  
Author(s):  
C. Zhu ◽  
K. Karplus ◽  
L. Grate ◽  
P. Coffino
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Budding Yeast ◽  
Yeast Saccharomyces Cerevisiae

scholarly journals Seg1 controls eisosome assembly and shape

2012 ◽  
Vol 198 (3) ◽  
pp. 405-420 ◽  
Author(s):  
Karen E. Moreira ◽  
Sebastian Schuck ◽  
Bianca Schrul ◽  
Florian Fröhlich ◽  
James B. Moseley ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Budding Yeast ◽  
Yeast Saccharomyces Cerevisiae ◽  
Normal Plasma ◽  
Cytoplasmic Proteins ◽  
Stable Domains

Eisosomes are stable domains at the plasma membrane of the budding yeast Saccharomyces cerevisiae and have been proposed to function in endocytosis. Eisosomes are composed of two main cytoplasmic proteins, Pil1 and Lsp1, that form a scaffold around furrow-like plasma membrane invaginations. We show here that the poorly characterized eisosome protein Seg1/Ymr086w is important for eisosome biogenesis and architecture. Seg1 was required for efficient incorporation of Pil1 into eisosomes and the generation of normal plasma membrane furrows. Seg1 preceded Pil1 during eisosome formation and established a platform for the assembly of other eisosome components. This platform was further shaped and stabilized upon the arrival of Pil1 and Lsp1. Moreover, Seg1 abundance controlled the shape of eisosomes by determining their length. Similarly, the Schizosaccharomyces pombe Seg1-like protein Sle1 was necessary to generate the filamentous eisosomes present in fission yeast. The function of Seg1 in the stepwise biogenesis of eisosomes reveals striking architectural similarities between eisosomes in yeast and caveolae in mammals.

scholarly journals The Schizosaccharomyces pombe homolog of Saccharomyces cerevisiae HAP2 reveals selective and stringent conservation of the small essential core protein domain.

1991 ◽  
Vol 11 (2) ◽  
pp. 611-619 ◽  
Author(s):  
J T Olesen ◽  
J D Fikes ◽  
L Guarente
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Transcriptional Activation ◽  
Core Protein ◽  
Protein Domain ◽  
Yeast Saccharomyces Cerevisiae ◽  
Acid Protein ◽  
Ccaat Box

The fission yeast Schizosaccharomyces pombe is immensely diverged from budding yeast (Saccharomyces cerevisiae) on an evolutionary time scale. We have used a fission yeast library to clone a homolog of S. cerevisiae HAP2, which along with HAP3 and HAP4 forms a transcriptional activation complex that binds to the CCAAT box. The S. pombe homolog php2 (S. pombe HAP2) was obtained by functional complementation in an S. cerevisiae hap2 mutant and retains the ability to associate with HAP3 and HAP4. We have previously demonstrated that the HAP2 subunit of the CCAAT-binding transcriptional activation complex from S. cerevisiae contains a 65-amino-acid "essential core" structure that is divisible into subunit association and DNA recognition domains. Here we show that Php2 contains a 60-amino-acid block that is 82% identical to this core. The remainder of the 334-amino-acid protein is completely without homology to HAP2. The function of php2 in S. pombe was investigated by disrupting the gene. Strikingly, like HAP2 in S. cerevisiae, the S. pombe gene is specifically involved in mitochondrial function. This contrasts to the situation in mammals, in which the homologous CCAAT-binding complex is a global transcriptional activator.

The Schizosaccharomyces pombe homolog of Saccharomyces cerevisiae HAP2 reveals selective and stringent conservation of the small essential core protein domain

1991 ◽  
Vol 11 (2) ◽  
pp. 611-619
Author(s):  
J T Olesen ◽  
J D Fikes ◽  
L Guarente
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Transcriptional Activation ◽  
Core Protein ◽  
Protein Domain ◽  
Yeast Saccharomyces Cerevisiae ◽  
Acid Protein ◽  
Ccaat Box

The fission yeast Schizosaccharomyces pombe is immensely diverged from budding yeast (Saccharomyces cerevisiae) on an evolutionary time scale. We have used a fission yeast library to clone a homolog of S. cerevisiae HAP2, which along with HAP3 and HAP4 forms a transcriptional activation complex that binds to the CCAAT box. The S. pombe homolog php2 (S. pombe HAP2) was obtained by functional complementation in an S. cerevisiae hap2 mutant and retains the ability to associate with HAP3 and HAP4. We have previously demonstrated that the HAP2 subunit of the CCAAT-binding transcriptional activation complex from S. cerevisiae contains a 65-amino-acid "essential core" structure that is divisible into subunit association and DNA recognition domains. Here we show that Php2 contains a 60-amino-acid block that is 82% identical to this core. The remainder of the 334-amino-acid protein is completely without homology to HAP2. The function of php2 in S. pombe was investigated by disrupting the gene. Strikingly, like HAP2 in S. cerevisiae, the S. pombe gene is specifically involved in mitochondrial function. This contrasts to the situation in mammals, in which the homologous CCAAT-binding complex is a global transcriptional activator.

scholarly journals CENP-A exceeds microtubule attachment sites in centromere clusters of both budding and fission yeast

2011 ◽  
Vol 195 (4) ◽  
pp. 563-572 ◽  
Author(s):  
Valerie C. Coffman ◽  
Pengcheng Wu ◽  
Mark R. Parthun ◽  
Jian-Qiu Wu
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Budding Yeast ◽  
Histone H3 ◽  
Kinetochore Assembly ◽  
Microtubule Attachment ◽  
Attachment Sites ◽  
Histone H3 Variant ◽  
Architectural Models

The stoichiometries of kinetochores and their constituent proteins in yeast and vertebrate cells were determined using the histone H3 variant CENP-A, known as Cse4 in budding yeast, as a counting standard. One Cse4-containing nucleosome exists in the centromere (CEN) of each chromosome, so it has been assumed that each anaphase CEN/kinetochore cluster contains 32 Cse4 molecules. We report that anaphase CEN clusters instead contained approximately fourfold more Cse4 in Saccharomyces cerevisiae and ∼40-fold more CENP-A (Cnp1) in Schizosaccharomyces pombe than predicted. These results suggest that the number of CENP-A molecules exceeds the number of kinetochore-microtubule (MT) attachment sites on each chromosome and that CENP-A is not the sole determinant of kinetochore assembly sites in either yeast. In addition, we show that fission yeast has enough Dam1–DASH complex for ring formation around attached MTs. The results of this study suggest the need for significant revision of existing CEN/kinetochore architectural models.

scholarly journals Budding yeast centromeric DNA and A+T rich bacterial DNA can function as centromeres in the fission yeast Schizosaccharomyces pombe

2019 ◽  
Author(s):  
Anne C Barbosa ◽  
Zhengyao Xu ◽  
Kazhal Karari ◽  
Silke Hauf ◽  
William RA Brown
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Dna Sequence ◽  
Budding Yeast ◽  
Bacterial Dna ◽  
Centromeric Dna ◽  
Serine Recombinases ◽  
Centromere Function ◽  
And Function

Eukaryotic centromeric DNA is famously variable in evolution but currently, this cannot be reconciled with the conservation of eukaryotic centromere function. It seems likely that centromeric DNA from different organisms contains conserved functionally important features but the identity of these features is unknown. The point centromeres of the budding yeast Saccharomyces cerevisiae and the regional centromeres of the fission yeast Schizosaccharomyces pombe are separated by 350 million years of evolution and are canonical examples of the paradoxical relationship1 between centromeric DNA sequence and function. We have established a centromere-replacement strategy in Schizosaccharomyces pombe in order to resolve this paradox experimentally. Centromere-replacement shows that an A+T rich bacterial DNA sequence has weak centromere function and that elements of the Saccharomyces cerevisiae centromere embedded in short sequences from the non-centromeric S. pombe wee1 gene function almost as well as native S. pombe centromeric DNA. These observations demonstrate that determinants of centromere function are held in common by the budding and fission yeasts and that A+T rich DNA is both necessary and sufficient for function in S. pombe. Given the evolutionary distance between these yeasts, it is likely that A+T rich DNA has centromere function in a wide variety of eukaryotes. Centromere-replacement uses unidirectional serine recombinases that work well in many organisms2 3 and our experimental strategy should allow this idea to be tested in other eukaryotes.

scholarly journals De Novo Biosynthesis of Vanillin in Fission Yeast (Schizosaccharomyces pombe) and Baker's Yeast (Saccharomyces cerevisiae)

2009 ◽  
Vol 75 (9) ◽  
pp. 2765-2774 ◽  
Author(s):  
Esben H. Hansen ◽  
Birger Lindberg Møller ◽  
Gertrud R. Kock ◽  
Camilla M. Bünner ◽  
Charlotte Kristensen ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
De Novo ◽  
Global Market ◽  
Baker’S Yeast ◽  
Yeast Cells ◽  
Vanillyl Alcohol ◽  
Baker's Yeast ◽  
Yeast Saccharomyces Cerevisiae

ABSTRACT Vanillin is one of the world's most important flavor compounds, with a global market of 180 million dollars. Natural vanillin is derived from the cured seed pods of the vanilla orchid (Vanilla planifolia), but most of the world's vanillin is synthesized from petrochemicals or wood pulp lignins. We have established a true de novo biosynthetic pathway for vanillin production from glucose in Schizosaccharomyces pombe, also known as fission yeast or African beer yeast, as well as in baker's yeast, Saccharomyces cerevisiae. Productivities were 65 and 45 mg/liter, after introduction of three and four heterologous genes, respectively. The engineered pathways involve incorporation of 3-dehydroshikimate dehydratase from the dung mold Podospora pauciseta, an aromatic carboxylic acid reductase (ACAR) from a bacterium of the Nocardia genus, and an O-methyltransferase from Homo sapiens. In S. cerevisiae, the ACAR enzyme required activation by phosphopantetheinylation, and this was achieved by coexpression of a Corynebacterium glutamicum phosphopantetheinyl transferase. Prevention of reduction of vanillin to vanillyl alcohol was achieved by knockout of the host alcohol dehydrogenase ADH6. In S. pombe, the biosynthesis was further improved by introduction of an Arabidopsis thaliana family 1 UDP-glycosyltransferase, converting vanillin into vanillin β-d-glucoside, which is not toxic to the yeast cells and thus may be accumulated in larger amounts. These de novo pathways represent the first examples of one-cell microbial generation of these valuable compounds from glucose. S. pombe yeast has not previously been metabolically engineered to produce any valuable, industrially scalable, white biotech commodity.

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.

scholarly journals Filamentous growth of the budding yeast Saccharomyces cerevisiae induced by overexpression of the WHI2 gene

Microbiology ◽  
1997 ◽  
Vol 143 (6) ◽  
pp. 1867-1876 ◽  
Author(s):  
P. A. Radcliffe ◽  
K. M. Binley ◽  
J. Trevethick ◽  
M. Hall ◽  
P. E. Sudbery
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Budding Yeast ◽  
Filamentous Growth ◽  
Yeast Saccharomyces Cerevisiae
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