Heteromer formation of a long-chain prenyl diphosphate synthase from fission yeast Dps1 and budding yeast Coq1*

The surfaces of flocculent and nonflocculent yeast cells have been examined by electron microscopy. Nonextractive preparative procedures for scanning electron microscopy allow comparison in which sharp or softened images of surface details (scars, etc.) are the criteria for relative abundance of flocculum material. Asexually flocculent budding-yeast cells cannot be distinguished from nonflocculent budding-yeast cells in scanning electron micrographs because the scar details of both are well resolved, being hard and sharp. On the other hand, flocculent fission-yeast cells are readily distinguished from nonflocculent cells because fission scars are mostly soft or obscured on flocculent cells, but sharp on nonflocculent cells. Sexually and asexually flocculent fission-yeast cells cannot be distinguished from one another as both are heavily clad in "mucilaginous" or "hairy" coverings. Examination of lightly extracted and heavily extracted flocculent fission-yeast cells by transmission electron microscopy provides micrographs consistent with the scanning electron micrographs.Key words: flocculation, budding yeast, fission yeast, scanning, transmission.

Download Full-text

Repeat-Associated Fission Yeast-Like Regional Centromeres in the Ascomycetous Budding Yeast Candida tropicalis

PLoS Genetics ◽

10.1371/journal.pgen.1005839 ◽

2016 ◽

Vol 12 (2) ◽

pp. e1005839 ◽

Cited By ~ 38

Author(s):

Gautam Chatterjee ◽

Sundar Ram Sankaranarayanan ◽

Krishnendu Guin ◽

Yogitha Thattikota ◽

Sreedevi Padmanabhan ◽

...

Keyword(s):

Fission Yeast ◽

Candida Tropicalis ◽

Budding Yeast

Download Full-text

Cleavage of Model Replication Forks by Fission Yeast Mus81-Eme1 and Budding Yeast Mus81-Mms4

Journal of Biological Chemistry ◽

10.1074/jbc.m210006200 ◽

2002 ◽

Vol 278 (9) ◽

pp. 6928-6935 ◽

Cited By ~ 85

Author(s):

Matthew C. Whitby ◽

Fekret Osman ◽

Julie Dixon

Keyword(s):

Fission Yeast ◽

Budding Yeast ◽

Replication Forks

Download Full-text

Functional Comparison of the Tup11 and Tup12 Transcriptional Corepressors in Fission Yeast

Molecular and Cellular Biology ◽

10.1128/mcb.25.2.716-727.2005 ◽

2005 ◽

Vol 25 (2) ◽

pp. 716-727 ◽

Cited By ~ 19

Author(s):

Fredrik Fagerström-Billai ◽

Anthony P. H. Wright

Keyword(s):

Gene Expression ◽

Gene Duplication ◽

Fission Yeast ◽

Budding Yeast ◽

Functional Difference ◽

Evolutionary Mechanism ◽

Genome Wide ◽

Number Of Genes ◽

Transcriptional Corepressors ◽

Genome Wide Gene Expression

ABSTRACT Gene duplication is considered an important evolutionary mechanism. Unlike many characterized species, the fission yeast Schizosaccharomyces pombe contains two paralogous genes, tup11 + and tup12 + , that encode transcriptional corepressors similar to the well-characterized budding yeast Tup1 protein. Previous reports have suggested that Tup11 and Tup12 proteins play redundant roles. Consistently, we show that the two Tup proteins can interact together when expressed at normal levels and that each can independently interact with the Ssn6 protein, as seen for Tup1 in budding yeast. However, tup11 − and tup12 − mutants have different phenotypes on media containing KCl and CaCl2. Consistent with the functional difference between tup11 − and tup12 − mutants, we identified a number of genes in genome-wide gene expression experiments that are differentially affected by mutations in the tup11 + and tup12 + genes. Many of these genes are differentially derepressed in tup11 − mutants and are over-represented in genes that have previously been shown to respond to a range of different stress conditions. Genes specifically derepressed in tup12 − mutants require the Ssn6 protein for their repression. As for Tup12, Ssn6 is also required for efficient adaptation to KCl- and CaCl2-mediated stress. We conclude that Tup11 and Tup12 are at least partly functionally diverged and suggest that the Tup12 and Ssn6 proteins have adopted a specific role in regulation of the stress response.

Download Full-text

Fission yeast Pds5 is required for accurate chromosome segregation and for survival after DNA damage or metaphase arrest

Journal of Cell Science ◽

10.1242/jcs.115.3.587 ◽

2002 ◽

Vol 115 (3) ◽

pp. 587-598 ◽

Cited By ~ 3

Author(s):

Shao-Win Wang ◽

Rebecca L. Read ◽

Chris J. Norbury

Keyword(s):

Dna Damage ◽

Fission Yeast ◽

Sister Chromatid ◽

Budding Yeast ◽

Eukaryotic Cell ◽

Sister Chromatid Cohesion ◽

Chromosome Loss ◽

Dependent Manner ◽

Yeast Saccharomyces Cerevisiae ◽

Chromatid Cohesion

Sister chromatid cohesion, which is established during the S phase of the eukaryotic cell cycle and persists until the onset of anaphase, is essential for the maintenance of genomic integrity. Cohesion requires the multi-protein complex cohesin, as well as a number of accessory proteins including Pds5/BIMD/Spo76. In the budding yeast Saccharomyces cerevisiae Pds5 is an essential protein that localises to chromosomes in a cohesin-dependent manner. Here we describe the characterisation in the fission yeast Schizosaccharomyces pombe of pds5+, a novel,non-essential orthologue of S. cerevisiae PDS5. The S. pombePds5 protein was localised to punctate nuclear foci in a manner that was dependent on the Rad21 cohesin component. This, together with additional genetic evidence, points towards an involvement of S. pombe Pds5 in sister chromatid cohesion. S. pombe pds5 mutants were hypersensitive to DNA damage and to mitotic metaphase delay, but this sensitivity was apparently not due to precocious loss of sister chromatid cohesion. These cells also suffered increased spontaneous chromosome loss and meiotic defects and their viability was dependent on the spindle checkpoint protein Bub1. Thus, while S. pombe Pds5 has an important cohesin-related role, this differs significantly from that of the equivalent budding yeast protein.

Download Full-text

The novel human protein serine/threonine phosphatase 6 is a functional homologue of budding yeast Sit4p and fission yeast ppe1, which are involved in cell cycle regulation

Journal of Cell Science ◽

10.1242/jcs.109.12.2865 ◽

1996 ◽

Vol 109 (12) ◽

pp. 2865-2874 ◽

Cited By ~ 1

Author(s):

H. Bastians ◽

H. Ponstingl

Keyword(s):

Cell Cycle ◽

Fission Yeast ◽

Shape Control ◽

Cell Cycle Regulation ◽

Budding Yeast ◽

Mitotic Checkpoint ◽

Human Protein ◽

Predicted Amino Acid Sequence ◽

Temperature Sensitive ◽

Cycle Regulation

We identified a novel human protein serine/threonine phosphatase cDNA, designated protein phosphatase 6 (PP6) by using a homology-based polymerase chain reaction. The predicted amino acid sequence indicates a 35 kDa protein showing high homology to other protein phosphatases including human PP2A (57%), human PP4 (59%), rat PPV (98%), Drosophila PPV (74%), Schizosaccharomyces pombe ppe1 (68%) and Saccharomyces cerevisiae Sit4p (61%). In human cells, three forms of PP6 mRNA were found with highest levels of expression in testis, heart and skeletal muscle. The PP6 protein was detected in lysates of human heart muscle and in bull testis. Complementation studies using a temperature sensitive mutant strain of S. cerevisiae SIT4, which is required for the G1 to S transition of the cell cycle, showed that PP6 can rescue the mutant growth arrest. In addition, a loss of function mutant of S. pombe ppe1, described as a gene interacting with the pim1/spi1 mitotic checkpoint and involved in cell shape control, can be complemented by expression of human PP6. These data indicate that human PP6 is a functional homologue of budding yeast Sit4p and fission yeast ppe1, implying a function of PP6 in cell cycle regulation.

Download Full-text

Assembly of fission yeast eisosomes in the plasma membrane of budding yeast: Import of foreign membrane microdomains

European Journal of Cell Biology ◽

10.1016/j.ejcb.2014.10.003 ◽

2015 ◽

Vol 94 (1) ◽

pp. 1-11 ◽

Cited By ~ 7

Author(s):

Katarina Vaskovicova ◽

Vendula Stradalova ◽

Ales Efenberk ◽

Miroslava Opekarova ◽

Jan Malinsky

Keyword(s):

Plasma Membrane ◽

Fission Yeast ◽

Budding Yeast ◽

Membrane Microdomains

Download Full-text

Multiple Orientation-Dependent, Synergistically Interacting, Similar Domains in the Ribosomal DNA Replication Origin of the Fission Yeast, Schizosaccharomyces pombe

Molecular and Cellular Biology ◽

10.1128/mcb.18.12.7294 ◽

1998 ◽

Vol 18 (12) ◽

pp. 7294-7303 ◽

Cited By ~ 40

Author(s):

Soo-Mi Kim ◽

Joel A. Huberman

Keyword(s):

Dna Replication ◽

Schizosaccharomyces Pombe ◽

Fission Yeast ◽

Ribosomal Dna ◽

Replication Origin ◽

Budding Yeast ◽

Sequence Motifs ◽

Dna Replication Origin ◽

Dna Replication Origins ◽

Origin Function

ABSTRACT Previous investigations have shown that the fission yeast,Schizosaccharomyces pombe, has DNA replication origins (500 to 1500 bp) that are larger than those in the budding yeast,Saccharomyces cerevisiae (100 to 150 bp). Deletion and linker substitution analyses of two fission yeast origins revealed that they contain multiple important regions with AT-rich asymmetric (abundant A residues in one strand and T residues in the complementary strand) sequence motifs. In this work we present the characterization of a third fission yeast replication origin, ars3001, which is relatively small (∼570 bp) and responsible for replication of ribosomal DNA. Like previously studied fission yeast origins,ars3001 contains multiple important regions. The three most important of these regions resemble each other in several ways: each region is essential for origin function and is at least partially orientation dependent, each region contains similar clusters of A+T-rich asymmetric sequences, and the regions can partially substitute for each other. These observations suggest that ars3001function requires synergistic interactions between domains binding similar proteins. It is likely that this requirement extends to other fission yeast origins, explaining why such origins are larger than those of budding yeast.

Download Full-text

Contribution of Alanine-76 and Serine Phosphorylation inα-Synuclein Membrane Association and Aggregation in Yeasts

Parkinson s Disease ◽

10.4061/2011/392180 ◽

2011 ◽

Vol 2011 ◽

pp. 1-12 ◽

Cited By ~ 8

Author(s):

Michael Fiske ◽

Stephanie Valtierra ◽

Keith Solvang ◽

Michael Zorniak ◽

Michael White ◽

...

Keyword(s):

Parkinson’S Disease ◽

Plasma Membrane ◽

Amino Acid ◽

Fission Yeast ◽

Dopaminergic Neurons ◽

Budding Yeast ◽

Serine Phosphorylation ◽

Membrane Association ◽

Midbrain Dopaminergic Neurons ◽

Substitution Mutations

In Parkinson's disease (PD), misfolded and aggregatedα-synuclein protein accumulates in degenerating midbrain dopaminergic neurons. The amino acid alanine-76 inα-synuclein and phosphorylation at serine-87 and serine-129 are thought to regulate its aggregation and toxicity. However, their exact contributions toα-synuclein membrane association are less clear. We found thatα-synuclein is indeed phosphorylated in fission yeast and budding yeast, the two models that we employed for assessingα-synuclein aggregation and membrane association properties, respectively. Surprisingly, blocking serine phosphorylation (S87A, S129A, and S87A/S129A) or mimicking it (S87D, S129D) alteredα-synuclein aggregation in fission yeast. Either blocking or mimicking this phosphorylation increased endomembrane association in fission yeast, but only mimicking it decreased plasma membrane association in budding yeast. Polar substitution mutations of alanine-76 (A76E and A76R) decreasedα-synuclein membrane association in budding yeast and decreased aggregation in fission yeast. These yeast studies extend our understanding of serine phosphorylation and alanine-76 contributions toα-synuclein aggregation and are the first to detail their impact onα-synuclein's plasma membrane and endomembrane association.

Download Full-text

Identification of a conserved F-box protein 6 interactor essential for endocytosis and cytokinesis in fission yeast

Biochemical Journal ◽

10.1042/bj20081659 ◽

2009 ◽

Vol 420 (2) ◽

pp. 169-180 ◽

Cited By ~ 9

Author(s):

Isabelle Jourdain ◽

Nathalie Spielewoy ◽

James Thompson ◽

Susheela Dhut ◽

John R. Yates ◽

...

Keyword(s):

Cell Division ◽

Fission Yeast ◽

Protein Identification ◽

Budding Yeast ◽

Affinity Purification ◽

Elongation Factor ◽

Temperature Sensitive ◽

Amino Acid Residues ◽

Lipid Kinase ◽

F Box Protein

The F-box domain is a degenerated motif consisting of ∼40 amino acid residues that specifically bind Skp1, a core component of the SCF (Skp1-Cdc53/Cullin 1-F-box protein) ubiquitin ligase. Recent work, mainly performed in budding yeast, indicates that certain F-box proteins form non-SCF complexes together with Skp1 in the absence of cullins and play various roles in cell cycle and signalling pathways. However, it is not established whether these non-SCF complexes are unique to budding yeast or common in other eukaryotes. In the present paper, using TAP (tandem affinity purification) coupled to MudPIT (Multidimensional Protein Identification Technology) analysis, we have identified a novel conserved protein, Sip1, in fission yeast, as an interacting partner of an essential F-box protein Pof6. Sip1 is a large HEAT (huntingtin, elongation factor 3, the PR65/A subunit of protein phosphatase 2A and the lipid kinase Tor)-repeats containing protein (217 kDa) and forms a complex with Pof6 and Skp1. This complex does not contain cullins, indicating that it is a novel non-SCF complex. Like Pof6 and Skp1, Sip1 is essential for cell viability and temperature-sensitive sip1 mutants display cell division arrest as binucleate cells with septa. Sip1 localizes to the nucleus and dynamic cytoplasmic dots, which are shown in the present study to be endocytic vesicles. Consistent with this, sip1 mutants are defective in endocytosis. Furthermore, towards the end of cytokinesis, constriction of the actomyosin ring and dissociation of type II myosin and septum materials are substantially delayed in the absence of functional Sip1. These results indicate that the conserved Sip1 protein comprises a novel non-SCF F-box complex that plays an essential role in endocytosis, cytokinesis and cell division.

Download Full-text