Organization, primary structure, and evolution of histone H2A and H2B genes of the fission yeast Schizosaccharomyces pombe.

The histone H2A and H2B genes of the fission yeast Schizosaccharomyces pombe were cloned and sequenced. Southern blot and sequence analyses showed that, unlike other eucaryotes, Saccharomyces cerevisiae included, S. pombe has unequal numbers of these genes, containing two histone H2A genes (H2A-alpha and -beta) and only one H2B gene (H2B-alpha) per haploid genome. H2A- and H2B-alpha are adjacent to each other and are divergently transcribed. H2A-beta has no other histone gene in close proximity. Preceding both H2A-alpha and -beta is a highly conserved 19-base-pair sequence (5'-CATCAC/AAACCCTAACCCTG-3'). The H2A DNA sequences encode two histone H2A subtypes differing in amino acid sequence (three residues) and size (H2A-alpha, 131 residues; H2A-beta, 130 residues). H2B-alpha codes for a 125-amino-acid protein. Sequence evolution is extensive between S. pombe and S. cerevisiae and displays unique patterns of divergence. Certain N-terminal sequences normally divergent between eucaryotes are conserved between the two yeasts. In contrast, the normally conserved hydrophobic core of H2A is as divergent between the yeasts as between S. pombe and calf.

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

Molecular and Cellular Biology ◽

10.1128/mcb.11.2.611 ◽

1991 ◽

Vol 11 (2) ◽

pp. 611-619 ◽

Cited By ~ 50

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.

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

Molecular and Cellular Biology ◽

10.1128/mcb.11.2.611-619.1991 ◽

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.

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Schizosaccharomyces pombe Vps34p, a phosphatidylinositol-specific PI 3-kinase essential for normal cell growth and vacuole morphology

Journal of Cell Science ◽

10.1242/jcs.108.12.3745 ◽

1995 ◽

Vol 108 (12) ◽

pp. 3745-3756 ◽

Cited By ~ 2

Author(s):

K. Takegawa ◽

D.B. DeWald ◽

S.D. Emr

Keyword(s):

Amino Acid ◽

Schizosaccharomyces Pombe ◽

Mammalian Cells ◽

Membrane Fraction ◽

Kinase Activity ◽

Temperature Sensitive ◽

Wild Type ◽

Phosphatidylinositol 3 Kinase ◽

Acid Protein ◽

Phosphatidylinositol 3

We have cloned the gene, vps34+, from the fission yeast Schizosaccharomyces pombe which encodes an 801 amino acid protein with phosphatidylinositol 3-kinase activity. The S. pombe Vps34 protein shares 43% amino acid sequence identity with the Saccharomyces cerevisiae Vps34 protein and 28% identity with the p110 catalytic subunit of the mammalian phosphatidylinositol 3-kinase. When the vps34+ gene is disrupted, S.pombe strains are temperature-sensitive for growth and the mutant cells contain enlarged vacuoles. Furthermore, while wild-type strains exhibit substantial levels of phosphatidylinositol 3-kinase activity, this activity is not detected in the vps34 delta strain. S.pombe Vps34p-specific antiserum detects a single protein in cells of -90 kDa that fractionates almost exclusively with the crude membrane fraction. Phosphatidylinositol 3-kinase activity also is localized mainly in the membrane fraction of wild-type cells. Immunoisolated Vps34p specifically phosphorylates phosphatidylinositol on the D-3 position of the inositol ring to yield phosphatidylinositol(3)phosphate. but does not utilize phosphatidylinositol(4)phosphate or phosphatidylinositol(4,5)bisphosphate as substrates. In addition, when compared to the mammalian p110 phosphatidylinositol 3-kinase, S. pombe Vps34p is relatively insensitive to the inhibitors wortmannin and LY294002. Together, these results indicate that S. pombe Vps34 is more similar to the phosphatidylinositol-specific 3-kinase, Vps34p from S. cerevisiae, and is distinct from the p110/p85 and G protein-coupled phosphatidylinositol 3-kinases from mammalian cells. These data are discussed in relation to the possible role of Vps34p in vesicle-mediated protein sorting to the S. pombe vacuole.

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Variables Influencing Differences in Sequence Conservation in the Fission Yeast Schizosaccharomyces pombe

Journal of Molecular Evolution ◽

10.1007/s00239-021-10028-y ◽

2021 ◽

Author(s):

Simon Emanuel Harnqvist ◽

Cooper Alastair Grace ◽

Daniel Charlton Jeffares

Keyword(s):

Schizosaccharomyces Pombe ◽

Fission Yeast ◽

Protein Interactions ◽

Model Organism ◽

Sequence Conservation ◽

Rate Variation ◽

Sequence Evolution ◽

Least Squares Regression ◽

Protein Protein Interactions ◽

Partial Correlations

AbstractWhich variables determine the constraints on gene sequence evolution is one of the most central questions in molecular evolution. In the fission yeast Schizosaccharomyces pombe, an important model organism, the variables influencing the rate of sequence evolution have yet to be determined. Previous studies in other single celled organisms have generally found gene expression levels to be most significant, with numerous other variables such as gene length and functional importance identified as having a smaller impact. Using publicly available data, we used partial least squares regression, principal components regression, and partial correlations to determine the variables most strongly associated with sequence evolution constraints. We identify centrality in the protein–protein interactions network, amino acid composition, and cellular location as the most important determinants of sequence conservation. However, each factor only explains a small amount of variance, and there are numerous variables having a significant or heterogeneous influence. Our models explain more than half of the variance in dN, raising the possibility that future refined models could quantify the role of stochastics in evolutionary rate variation.

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Human p53 inhibits growth in Schizosaccharomyces pombe

Molecular and Cellular Biology ◽

10.1128/mcb.12.4.1405-1411.1992 ◽

1992 ◽

Vol 12 (4) ◽

pp. 1405-1411

Author(s):

J R Bischoff ◽

D Casso ◽

D Beach

Keyword(s):

Amino Acid ◽

Schizosaccharomyces Pombe ◽

Fission Yeast ◽

Amino Acid Residue ◽

Mechanism Of Action ◽

Mammalian Cells ◽

Simple System ◽

Wild Type ◽

Dominant Mutation ◽

Mutant Forms

Overexpression of wild-type p53 in mammalian cells blocks growth. We show here that the overexpression of wild-type human p53 in the fission yeast Schizosaccharomyces pombe also blocks growth, whereas the overexpression of mutant forms of p53 does not. The p53 polypeptide is located in the nucleus and is phosphorylated at both the cdc2 site and the casein kinase II site in S. pombe. A new dominant mutation of p53, resulting in the change of a cysteine to an arginine at amino acid residue 141, was identified. The results presented here demonstrate that S. pombe could provide a simple system for studying the mechanism of action of human p53.

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Multiple drug resistance in the fission yeast Schizosaccharomyces pombe: Correlation between drug and amino acid uptake and membrane ATPase activities

Current Genetics ◽

10.1007/bf00376075 ◽

1983 ◽

Vol 7 (4) ◽

pp. 299-307 ◽

Cited By ~ 9

Author(s):

Paul A. Johnston ◽

Alan Coddington

Keyword(s):

Drug Resistance ◽

Amino Acid ◽

Schizosaccharomyces Pombe ◽

Fission Yeast ◽

Multiple Drug Resistance ◽

Amino Acid Uptake ◽

Multiple Drug ◽

Acid Uptake ◽

Membrane Atpase

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Structural organization and functional analysis of centromeric DNA in the fission yeast Schizosaccharomyces pombe

Molecular and Cellular Biology ◽

10.1128/mcb.8.2.754-763.1988 ◽

1988 ◽

Vol 8 (2) ◽

pp. 754-763

Author(s):

B Fishel ◽

H Amstutz ◽

M Baum ◽

J Carbon ◽

L Clarke

Keyword(s):

Schizosaccharomyces Pombe ◽

Fission Yeast ◽

Dna Sequences ◽

Centromeric Dna ◽

Centromere Function ◽

Leu2 Gene ◽

Centromeric Repeat ◽

Sequence Elements ◽

Chromosome Iii ◽

Chromosome Ii

Centromeric DNA in the fission yeast Schizosaccharomyces pombe was isolated by chromosome walking and by field inversion gel electrophoretic fractionation of large genomic DNA restriction fragments. The centromere regions of the three chromosomes were contained on three SalI fragments (120 kilobases [kb], chromosome III; 90 kb, chromosome II; and 50 kb, chromosome I). Each fragment contained several repetitive DNA sequences, including repeat K (6.4 kb), repeat L (6.0 kb), and repeat B, that occurred only in the three centromere regions. On chromosome II, these repeats were organized into a 35-kb inverted repeat that included one copy of K and L in each arm of the repeat. Site-directed integration of a plasmid containing the yeast LEU2 gene into K repeats at each of the centromeres or integration of an intact K repeat into a chromosome arm had no effect on mitotic or meiotic centromere function. The centromeric repeat sequences were not transcribed and possessed many of the properties of constitutive heterochromatin. Thus, S. pombe is an excellent model system for studies on the role of repetitive sequence elements in centromere function.

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