Regional control of histone H3 lysine 27 methylation in Neurospora

Trimethylated lysine 27 on histone H3 (H3K27me3) is present in Drosophila, Arabidopsis. worms, and mammals, but is absent from yeasts that have been examined. We identified and analyzed H3K27me3 in the filamentous fungus Neurospora crassa and in other Neurospora species. H3K27me3 covers 6.8% of the...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 110; no. 15; pp. 6027 - 6032
Main Authors Jamieson, Kirsty, Rountree, Michael R., Lewis, Zachary A., Stajich, Jason E., Selker, Eric U.
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 09.04.2013
National Acad Sciences
Subjects
Arabidopsis
Biological Sciences
Catalytic Domain
Chromatin
Cluster Analysis
Computational Biology
DNA
DNA methylation
Drosophila
Epigenesis, Genetic
Epigenetics
Fungi
Gene Deletion
gene expression regulation
Gene Expression Regulation, Fungal
Genes
Genetic markers
Genome, Fungal
Genomes
Histones
Histones - genetics
Insects
lysine
Lysine - metabolism
mammals
Markov Chains
Methylation
Neurospora
Neurospora - genetics
Neurospora - metabolism
Neurospora crassa
Sequence Analysis, DNA
Telomeres
transcription (genetics)
Yeasts
Online AccessGet full text
ISSN0027-8424
1091-6490
1091-6490
DOI10.1073/pnas.1303750110

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Abstract Trimethylated lysine 27 on histone H3 (H3K27me3) is present in Drosophila, Arabidopsis. worms, and mammals, but is absent from yeasts that have been examined. We identified and analyzed H3K27me3 in the filamentous fungus Neurospora crassa and in other Neurospora species. H3K27me3 covers 6.8% of the N. crassa genome, encompassing 223 domains, including 774 genes, all of which are transcriptionally silent N. crassa H3K27me3-marked genes are less conserved than unmarked genes and only ~35% of genes marked by H3K27me3 in N. crassa are also H3K27me3-marked in Neurospora discreta and Neurospora tetrasperma. We found that three components of the Neurospora Polycomb repressive complex 2 (PRC2)—[Su-(var) 3-9; E(z); Trrthorax] (SET)-7, embryonic ectoderm development (EED), and SU(Z)12 (suppressor of zeste12)—are required for H3K27me3, whereas the fourth component Neurospora protein 55 (an N. crassa homolog of p55/RbAp48), is critical for H3K27me3 only at subtelomeric domains. Loss of H3K27me3, caused by deletion of the gene encoding the catalytic PRC2 subunit, set-7, resulted in up-regulation of 130 genes, including genes in both H3K27me3-marked and unmarked regions.
AbstractList Trimethylated lysine 27 on histone H3 (H3K27me3) is present in Drosophila, Arabidopsis, worms, and mammals, but is absent from yeasts that have been examined. We identified and analyzed H3K27me3 in the filamentous fungus Neurospora crassa and in other Neurospora species. H3K27me3 covers 6.8% of the N. crassa genome, encompassing 223 domains, including 774 genes, all of which are transcriptionally silent. N. crassa H3K27me3-marked genes are less conserved than unmarked genes and only ~35% of genes marked by H3K27me3 in N. crassa are also H3K27me3-marked in Neurospora discreta and Neurospora tetrasperma. We found that three components of the Neurospora Polycomb repressive complex 2 (PRC2)-[Su-(var)3-9; E(z); Trithorax] (SET)-7, embryonic ectoderm development (EED), and SU(Z)12 (suppressor of zeste12) -- are required for H3K27me3, whereas the fourth component, Neurospora protein 55 (an N. crassa homolog of p55/RbAp48), is critical for H3K27me3 only at subtelomeric domains. Loss of H3K27me3, caused by deletion of the gene encoding the catalytic PRC2 subunit, set-7, resulted in up-regulation of 130 genes, including genes in both H3K27me3-marked and unmarked regions. [PUBLICATION ABSTRACT]
Trimethylated lysine 27 on histone H3 (H3K27me3) is present in Drosophila, Arabidopsis , worms, and mammals, but is absent from yeasts that have been examined. We identified and analyzed H3K27me3 in the filamentous fungus Neurospora crassa and in other Neurospora species. H3K27me3 covers 6.8% of the N. crassa genome, encompassing 223 domains, including 774 genes, all of which are transcriptionally silent. N. crassa H3K27me3-marked genes are less conserved than unmarked genes and only ∼35% of genes marked by H3K27me3 in N. crassa are also H3K27me3-marked in Neurospora discreta and Neurospora tetrasperma . We found that three components of the Neurospora Polycomb repressive complex 2 (PRC2)—[Su-(var)3–9; E(z); Trithorax] (SET)-7, embryonic ectoderm development (EED), and SU(Z)12 (suppressor of zeste12)—are required for H3K27me3, whereas the fourth component, Neurospora protein 55 (an N. crassa homolog of p55/RbAp48), is critical for H3K27me3 only at subtelomeric domains. Loss of H3K27me3, caused by deletion of the gene encoding the catalytic PRC2 subunit, set-7 , resulted in up-regulation of 130 genes, including genes in both H3K27me3-marked and unmarked regions.
Trimethylated lysine 27 on histone H3 (H3K27me3) is present in Drosophila, Arabidopsis , worms, and mammals, but is absent from yeasts that have been examined. We identified and analyzed H3K27me3 in the filamentous fungus Neurospora crassa and in other Neurospora species. H3K27me3 covers 6.8% of the N. crassa genome, encompassing 223 domains, including 774 genes, all of which are transcriptionally silent. N. crassa H3K27me3-marked genes are less conserved than unmarked genes and only ∼35% of genes marked by H3K27me3 in N. crassa are also H3K27me3-marked in Neurospora discreta and Neurospora tetrasperma . We found that three components of the Neurospora Polycomb repressive complex 2 (PRC2)—[Su-(var)3–9; E(z); Trithorax] (SET)-7, embryonic ectoderm development (EED), and SU(Z)12 (suppressor of zeste12)—are required for H3K27me3, whereas the fourth component, Neurospora protein 55 (an N. crassa homolog of p55/RbAp48), is critical for H3K27me3 only at subtelomeric domains. Loss of H3K27me3, caused by deletion of the gene encoding the catalytic PRC2 subunit, set-7 , resulted in up-regulation of 130 genes, including genes in both H3K27me3-marked and unmarked regions.
Trimethylated lysine 27 on histone H3 (H3K27me3) is present in Drosophila, Arabidopsis, worms, and mammals, but is absent from yeasts that have been examined. We identified and analyzed H3K27me3 in the filamentous fungus Neurospora crassa and in other Neurospora species. H3K27me3 covers 6.8% of the N. crassa genome, encompassing 223 domains, including 774 genes, all of which are transcriptionally silent. N. crassa H3K27me3-marked genes are less conserved than unmarked genes and only ∼35% of genes marked by H3K27me3 in N. crassa are also H3K27me3-marked in Neurospora discreta and Neurospora tetrasperma. We found that three components of the Neurospora Polycomb repressive complex 2 (PRC2)--[Su-(var)3-9; E(z); Trithorax] (SET)-7, embryonic ectoderm development (EED), and SU(Z)12 (suppressor of zeste12)--are required for H3K27me3, whereas the fourth component, Neurospora protein 55 (an N. crassa homolog of p55/RbAp48), is critical for H3K27me3 only at subtelomeric domains. Loss of H3K27me3, caused by deletion of the gene encoding the catalytic PRC2 subunit, set-7, resulted in up-regulation of 130 genes, including genes in both H3K27me3-marked and unmarked regions.Trimethylated lysine 27 on histone H3 (H3K27me3) is present in Drosophila, Arabidopsis, worms, and mammals, but is absent from yeasts that have been examined. We identified and analyzed H3K27me3 in the filamentous fungus Neurospora crassa and in other Neurospora species. H3K27me3 covers 6.8% of the N. crassa genome, encompassing 223 domains, including 774 genes, all of which are transcriptionally silent. N. crassa H3K27me3-marked genes are less conserved than unmarked genes and only ∼35% of genes marked by H3K27me3 in N. crassa are also H3K27me3-marked in Neurospora discreta and Neurospora tetrasperma. We found that three components of the Neurospora Polycomb repressive complex 2 (PRC2)--[Su-(var)3-9; E(z); Trithorax] (SET)-7, embryonic ectoderm development (EED), and SU(Z)12 (suppressor of zeste12)--are required for H3K27me3, whereas the fourth component, Neurospora protein 55 (an N. crassa homolog of p55/RbAp48), is critical for H3K27me3 only at subtelomeric domains. Loss of H3K27me3, caused by deletion of the gene encoding the catalytic PRC2 subunit, set-7, resulted in up-regulation of 130 genes, including genes in both H3K27me3-marked and unmarked regions.
Trimethylated lysine 27 on histone H3 (H3K27me3) is present in Drosophila, Arabidopsis. worms, and mammals, but is absent from yeasts that have been examined. We identified and analyzed H3K27me3 in the filamentous fungus Neurospora crassa and in other Neurospora species. H3K27me3 covers 6.8% of the N. crassa genome, encompassing 223 domains, including 774 genes, all of which are transcriptionally silent N. crassa H3K27me3-marked genes are less conserved than unmarked genes and only ~35% of genes marked by H3K27me3 in N. crassa are also H3K27me3-marked in Neurospora discreta and Neurospora tetrasperma. We found that three components of the Neurospora Polycomb repressive complex 2 (PRC2)—[Su-(var) 3-9; E(z); Trrthorax] (SET)-7, embryonic ectoderm development (EED), and SU(Z)12 (suppressor of zeste12)—are required for H3K27me3, whereas the fourth component Neurospora protein 55 (an N. crassa homolog of p55/RbAp48), is critical for H3K27me3 only at subtelomeric domains. Loss of H3K27me3, caused by deletion of the gene encoding the catalytic PRC2 subunit, set-7, resulted in up-regulation of 130 genes, including genes in both H3K27me3-marked and unmarked regions.
Author Stajich, Jason E.
Rountree, Michael R.
Lewis, Zachary A.
Selker, Eric U.
Jamieson, Kirsty
Author_xml – sequence: 1
  givenname: Kirsty
  surname: Jamieson
  fullname: Jamieson, Kirsty
– sequence: 2
  givenname: Michael R.
  surname: Rountree
  fullname: Rountree, Michael R.
– sequence: 3
  givenname: Zachary A.
  surname: Lewis
  fullname: Lewis, Zachary A.
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  givenname: Jason E.
  surname: Stajich
  fullname: Stajich, Jason E.
– sequence: 5
  givenname: Eric U.
  surname: Selker
  fullname: Selker, Eric U.
BackLink https://www.ncbi.nlm.nih.gov/pubmed/23530226$$D View this record in MEDLINE/PubMed
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ISSN 0027-8424
1091-6490
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2Present address: Department of Microbiology, University of Georgia, Athens, GA 30602.
Author contributions: K.J., M.R.R., Z.A.L., J.E.S., and E.U.S. designed research; K.J., M.R.R., Z.A.L., J.E.S., and E.U.S. performed research; K.J., M.R.R., Z.A.L., J.E.S., and E.U.S. contributed new reagents/analytic tools; K.J., M.R.R., Z.A.L., J.E.S., and E.U.S. analyzed data; and K.J., M.R.R., and E.U.S. wrote the paper.
1K.J. and M.R.R. contributed equally to this work.
Contributed by Eric U. Selker, February 27, 2013 (sent for review February 11, 2013)
OpenAccessLink https://www.pnas.org/content/pnas/110/15/6027.full.pdf
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Snippet Trimethylated lysine 27 on histone H3 (H3K27me3) is present in Drosophila, Arabidopsis. worms, and mammals, but is absent from yeasts that have been examined....
Trimethylated lysine 27 on histone H3 (H3K27me3) is present in Drosophila, Arabidopsis , worms, and mammals, but is absent from yeasts that have been examined....
Trimethylated lysine 27 on histone H3 (H3K27me3) is present in Drosophila, Arabidopsis , worms, and mammals, but is absent from yeasts that have been examined....
Trimethylated lysine 27 on histone H3 (H3K27me3) is present in Drosophila, Arabidopsis, worms, and mammals, but is absent from yeasts that have been examined....
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SourceType Open Access Repository
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Index Database
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StartPage 6027
SubjectTerms Arabidopsis
Biological Sciences
Catalytic Domain
Chromatin
Cluster Analysis
Computational Biology
DNA
DNA methylation
Drosophila
Epigenesis, Genetic
Epigenetics
Fungi
Gene Deletion
gene expression regulation
Gene Expression Regulation, Fungal
Genes
Genetic markers
Genome, Fungal
Genomes
Histones
Histones - genetics
Insects
lysine
Lysine - metabolism
mammals
Markov Chains
Methylation
Neurospora
Neurospora - genetics
Neurospora - metabolism
Neurospora crassa
Sequence Analysis, DNA
Telomeres
transcription (genetics)
Yeasts
Title Regional control of histone H3 lysine 27 methylation in Neurospora
URI https://www.jstor.org/stable/42590348
http://www.pnas.org/content/110/15/6027.abstract
https://www.ncbi.nlm.nih.gov/pubmed/23530226
https://www.proquest.com/docview/1326429785
https://www.proquest.com/docview/1326143552
https://www.proquest.com/docview/1803141761
https://pubmed.ncbi.nlm.nih.gov/PMC3625340
Volume 110
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