Histone H3 lysine-to-methionine mutants as a paradigm to study chromatin signaling
Histone H3 lysine27-to-methionine (H3K27M) gain-of-function mutations occur in highly aggressive pediatric gliomas. We established a Drosophila animal model for the pathogenic histone H3K27M mutation and show that its overexpression resembles polycomb repressive complex 2 (PRC2) loss-of-function phe...
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| Published in | Science (American Association for the Advancement of Science) Vol. 345; no. 6200; pp. 1065 - 1070 |
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| Main Authors | , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
American Association for the Advancement of Science
29.08.2014
The American Association for the Advancement of Science |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Histone H3 lysine27-to-methionine (H3K27M) gain-of-function mutations occur in highly aggressive pediatric gliomas. We established a Drosophila animal model for the pathogenic histone H3K27M mutation and show that its overexpression resembles polycomb repressive complex 2 (PRC2) loss-of-function phenotypes, causing derepression of PRC2 target genes and developmental perturbations. Similarly, an H3K9Mmutant depletes H3K9methylation levels and suppresses position-effect variegation in various Drosophila tissues.The histone H3K9 demethylase KDM3B/JHDM2 associates with H3K9M-containing nucleosomes, and its misregulation in Drosophila results in changes of H3K9 methylation levels and heterochromatic silencing defects. We have established histone lysine-to-methionine mutants as robust in vivo tools for inhibiting methylation pathways that also function as biochemical reagents for capturing site-specific histone-modifying enzymes, thus providing molecular insight into chromatin signaling pathways. |
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| AbstractList | Chromatin mutations disrupt developmentHistone proteins form the core packaging material for our genomic DNA, and covalent modifications to amino acid residues in their structure play an important role in the epigenetic control of gene expression. Herz et al. show that specific mutations in the residues that are normally modified to regulate expression cause severe disruption of normal development in the fruit fly. Similar mutations are known to be involved in a subtype of aggressive pediatric brain cancers. Insights into the epigenetic regulatory pathways disrupted by these mutations in Drosophila may suggest possible treatments for human cancers.Science, this issue p. 1065 Histone H3 lysine27-to-methionine (H3K27M) gain-of-function mutations occur in highly aggressive pediatric gliomas. We established a Drosophila animal model for the pathogenic histone H3K27M mutation and show that its overexpression resembles polycomb repressive complex 2 (PRC2) loss-of-function phenotypes, causing derepression of PRC2 target genes and developmental perturbations. Similarly, an H3K9Mmutant depletes H3K9methylation levels and suppresses position-effect variegation in various Drosophila tissues.The histone H3K9 demethylase KDM3B/JHDM2 associates with H3K9M-containing nucleosomes, and its misregulation in Drosophila results in changes of H3K9 methylation levels and heterochromatic silencing defects. We have established histone lysine-to-methionine mutants as robust in vivo tools for inhibiting methylation pathways that also function as biochemical reagents for capturing site-specific histone-modifying enzymes, thus providing molecular insight into chromatin signaling pathways. Histone H3 lysine27-to-methionine (H3K27M) gain-of-function mutations occur in highly aggressive pediatric gliomas. Here, we establish a Drosophila animal model for the pathogenic histone H3K27M mutation and show that its overexpression resembles Polycomb repressive complex 2 (PRC2) loss-of-function phenotypes, causing de-repression of PRC2 target genes and developmental perturbations. Similarly, a H3K9M mutant depletes H3K9 methylation levels and suppresses position-effect variegation in various Drosophila tissues. The histone H3K9 demethylase KDM3B/JHDM2 associates with H3K9M nucleosomes and its overexpression in Drosophila results in loss of H3K9 methylation levels and heterochromatic silencing defects. Here we establish histone lysine-to-methionine mutants as robust in vivo tools for inhibiting methylation pathways that also function as biochemical reagents for capturing site-specific histone-modifying enzymes, thus providing molecular insight into chromatin-signaling pathways. Histone proteins form the core packaging material for our genomic DNA, and covalent modifications to amino acid residues in their structure play an important role in the epigenetic control of gene expression. Herz et al. show that specific mutations in the residues that are normally modified to regulate expression cause severe disruption of normal development in the fruit fly. Similar mutations are known to be involved in a subtype of aggressive pediatric brain cancers. Insights into the epigenetic regulatory pathways disrupted by these mutations in Drosophila may suggest possible treatments for human cancers.; Science, this issue p. 1065 [PUBLICATION ABSTRACT] Histone H3 lysine27-to-methionine (H3K27M) gain-of-function mutations occur in highly aggressive pediatric gliomas. We established a Drosophila animal model for the pathogenic histone H3K27M mutation and show that its overexpression resembles polycomb repressive complex 2 (PRC2) loss-of-function phenotypes, causing derepression of PRC2 target genes and developmental perturbations. Similarly, an H3K9M mutant depletes H3K9 methylation levels and suppresses position-effect variegation in various Drosophila tissues. The histone H3K9 demethylase KDM3B/JHDM2 associates with H3K9M-containing nucleosomes, and its misregulation in Drosophila results in changes of H3K9 methylation levels and heterochromatic silencing defects. We have established histone lysine-to-methionine mutants as robust in vivo tools for inhibiting methylation pathways that also function as biochemical reagents for capturing site-specific histone-modifying enzymes, thus providing molecular insight into chromatin signaling pathways. [PUBLICATION ABSTRACT] Chromatin mutations disrupt development Histone proteins form the core packaging material for our genomic DNA, and covalent modifications to amino acid residues in their structure play an important role in the epigenetic control of gene expression. Herz et al. show that specific mutations in the residues that are normally modified to regulate expression cause severe disruption of normal development in the fruit fly. Similar mutations are known to be involved in a subtype of aggressive pediatric brain cancers. Insights into the epigenetic regulatory pathways disrupted by these mutations in Drosophila may suggest possible treatments for human cancers. Science , this issue p. 1065 Mutations in the DNA packaging material disrupt fruit fly development and reveal epigenetic regulatory pathways. Histone H3 lysine 27 -to-methionine (H3K27M) gain-of-function mutations occur in highly aggressive pediatric gliomas. We established a Drosophila animal model for the pathogenic histone H3K27M mutation and show that its overexpression resembles polycomb repressive complex 2 (PRC2) loss-of-function phenotypes, causing derepression of PRC2 target genes and developmental perturbations. Similarly, an H3K9M mutant depletes H3K9 methylation levels and suppresses position-effect variegation in various Drosophila tissues. The histone H3K9 demethylase KDM3B/JHDM2 associates with H3K9M-containing nucleosomes, and its misregulation in Drosophila results in changes of H3K9 methylation levels and heterochromatic silencing defects. We have established histone lysine-to-methionine mutants as robust in vivo tools for inhibiting methylation pathways that also function as biochemical reagents for capturing site-specific histone-modifying enzymes, thus providing molecular insight into chromatin signaling pathways. Histone H3 lysine(27)-to-methionine (H3K27M) gain-of-function mutations occur in highly aggressive pediatric gliomas. We established a Drosophila animal model for the pathogenic histone H3K27M mutation and show that its overexpression resembles polycomb repressive complex 2 (PRC2) loss-of-function phenotypes, causing derepression of PRC2 target genes and developmental perturbations. Similarly, an H3K9M mutant depletes H3K9 methylation levels and suppresses position-effect variegation in various Drosophila tissues. The histone H3K9 demethylase KDM3B/JHDM2 associates with H3K9M-containing nucleosomes, and its misregulation in Drosophila results in changes of H3K9 methylation levels and heterochromatic silencing defects. We have established histone lysine-to-methionine mutants as robust in vivo tools for inhibiting methylation pathways that also function as biochemical reagents for capturing site-specific histone-modifying enzymes, thus providing molecular insight into chromatin signaling pathways. |
| Author | Jackson, Jessica Gao, Xin Herz, Hans-Martin Florens, Laurence Shilatifard, Ali Rickels, Ryan Washburn, Michael P. Morgan, Marc Swanson, Selene K. Eissenberg, Joel C. |
| AuthorAffiliation | 1 Stowers Institute for Medical Research, 1000 East 50 th Street, Kansas City, MO 64110 3 Department of Pathology and Laboratory Medicine, University of Kansas Medical Center, Kansas City, Kansas 66160, USA 2 Saint Louis University School of Medicine, Edward A. Doisy Department of Biochemistry and Molecular Biology, St. Louis, MO |
| AuthorAffiliation_xml | – name: 2 Saint Louis University School of Medicine, Edward A. Doisy Department of Biochemistry and Molecular Biology, St. Louis, MO – name: 3 Department of Pathology and Laboratory Medicine, University of Kansas Medical Center, Kansas City, Kansas 66160, USA – name: 1 Stowers Institute for Medical Research, 1000 East 50 th Street, Kansas City, MO 64110 |
| Author_xml | – sequence: 1 givenname: Hans-Martin surname: Herz fullname: Herz, Hans-Martin – sequence: 2 givenname: Marc surname: Morgan fullname: Morgan, Marc – sequence: 3 givenname: Xin surname: Gao fullname: Gao, Xin – sequence: 4 givenname: Jessica surname: Jackson fullname: Jackson, Jessica – sequence: 5 givenname: Ryan surname: Rickels fullname: Rickels, Ryan – sequence: 6 givenname: Selene K. surname: Swanson fullname: Swanson, Selene K. – sequence: 7 givenname: Laurence surname: Florens fullname: Florens, Laurence – sequence: 8 givenname: Michael P. surname: Washburn fullname: Washburn, Michael P. – sequence: 9 givenname: Joel C. surname: Eissenberg fullname: Eissenberg, Joel C. – sequence: 10 givenname: Ali surname: Shilatifard fullname: Shilatifard, Ali |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/25170156$$D View this record in MEDLINE/PubMed |
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| Snippet | Histone H3 lysine27-to-methionine (H3K27M) gain-of-function mutations occur in highly aggressive pediatric gliomas. We established a Drosophila animal model... Histone H3 lysine(27)-to-methionine (H3K27M) gain-of-function mutations occur in highly aggressive pediatric gliomas. We established a Drosophila animal model... Chromatin mutations disrupt development Histone proteins form the core packaging material for our genomic DNA, and covalent modifications to amino acid... Histone proteins form the core packaging material for our genomic DNA, and covalent modifications to amino acid residues in their structure play an important... Chromatin mutations disrupt developmentHistone proteins form the core packaging material for our genomic DNA, and covalent modifications to amino acid residues... Histone H3 lysine27-to-methionine (H3K27M) gain-of-function mutations occur in highly aggressive pediatric gliomas. Here, we establish a Drosophila animal... |
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| SubjectTerms | Aggression Amino Acid Substitution Amino acids Animals Brain Chromatin Chromatin - metabolism Covalence Disease Models, Animal Drosophila Drosophila melanogaster Drosophila Proteins - genetics Epigenetics Fruits Gene expression Gene Silencing Glioma - genetics Glioma - metabolism Government regulations Heterochromatin - metabolism Histone-Lysine N-Methyltransferase - genetics Histones Histones - genetics Histones - metabolism Jumonji Domain-Containing Histone Demethylases - metabolism Lysine - genetics Methionine - genetics Methylation Mutation Mutations Proteins Residues Signal Transduction |
| Title | Histone H3 lysine-to-methionine mutants as a paradigm to study chromatin signaling |
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