PatentDOI
Histone demethylation mediated by the nuclear amine oxidase homolog lsd1
Yang Shi,Yujiang Shi +1 more
TLDR
In this paper, the authors identify a histone demethylase conserved from S. pombe to human and reveal dynamic regulation of histone methylation by both histonemethylases and demethylases.About:
This article is published in Cell.The article was published on 2005-12-16. It has received 3281 citations till now. The article focuses on the topics: Histone lysine demethylation & Histone demethylation.read more
Citations
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Journal ArticleDOI
Functional Role of G9a Histone Methyltransferase in Cancer
TL;DR: In this article, the role of G9a, a histone methyltransferase responsible for histone H3 lysine 9 (H3K9) mono-and dimethylation, is discussed, focusing on its functional role in regulating gene expression as well as its implications in cancer initiation and progression.
Journal ArticleDOI
Ubp10/Dot4p Regulates the Persistence of Ubiquitinated Histone H2B: Distinct Roles in Telomeric Silencing and General Chromatin
TL;DR: It is proposed that Ubp10p and Ubp8p are the only ubiquitin proteases that normally remove monoubiquitin from histone H2B and, while there are regions of the genome to which each is specifically targeted, both combine to regulate the global balance of H 2B ubiquitination.
Journal ArticleDOI
Histone methylation makes its mark on longevity.
Shuo Han,Anne Brunet +1 more
TL;DR: The epigenetic regulation of lifespan in diverse model organisms is described, focusing on the role and mode of action of chromatin regulators that affect two epigenetic marks, trimethylated lysine 4 of histone H3 (H3K4me3) and trimethylator 27 of hist one H2 (H2K27me3), in longevity.
Journal ArticleDOI
The tale of two domains: proteomics and genomics analysis of SMYD2, a new histone methyltransferase.
Mohamed Abu-Farha,Jean-Philippe Lambert,Ashraf S. Al-Madhoun,Fred Elisma,Ilona S. Skerjanc,Daniel Figeys +5 more
TL;DR: The combination of the SMYD2 interactome with the gene expression data suggests that some of the genes regulated bySMYD2 are closely associated with SMYD1-interacting proteins.
Journal ArticleDOI
Dynamic epigenetic regulation in neurons: enzymes, stimuli and signaling pathways
TL;DR: This Review discusses how extracellular cues, including synaptic activity and neurotrophic factors, influence epigenetic modifications and regulate the neuronal transcriptional response and summarizes additional mechanisms that induce chromatin remodeling events by combinatorial assembly of multiprotein complexes on neuronal gene promoters.
References
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Journal ArticleDOI
Translating the Histone Code
Thomas Jenuwein,C. David Allis +1 more
TL;DR: It is proposed that this epigenetic marking system represents a fundamental regulatory mechanism that has an impact on most, if not all, chromatin-templated processes, with far-reaching consequences for cell fate decisions and both normal and pathological development.
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Role of Histone H3 Lysine 27 Methylation in Polycomb-Group Silencing
Ru Cao,Liangjun Wang,Hengbin Wang,Li Xia,Hediye Erdjument-Bromage,Paul Tempst,Richard S. Jones,Yi Zhang +7 more
TL;DR: The purification and characterization of an EED-EZH2 complex, the human counterpart of the Drosophila ESC-E(Z) complex, is reported, and it is demonstrated that the complex specifically methylates nucleosomal histone H3 at lysine 27 (H3-K27).
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Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins.
TL;DR: It is shown that mammalian methyltransferases that selectively methylate histone H3 on lysine 9 (Suv39h HMTases) generate a binding site for HP1 proteins—a family of heterochromatic adaptor molecules implicated in both gene silencing and supra-nucleosomal chromatin structure.
Journal ArticleDOI
Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain.
Andrew J. Bannister,Philip Zegerman,Janet F. Partridge,Eric A. Miska,Jean O. Thomas,Robin C. Allshire,Tony Kouzarides +6 more
TL;DR: A stepwise model for the formation of a transcriptionally silent heterochromatin is provided: SUV39H1 places a ‘methyl marker’ on histone H3, which is then recognized by HP1 through its chromo domain, which may also explain the stable inheritance of theheterochromatic state.
Journal ArticleDOI
Regulation of chromatin structure by site-specific histone H3 methyltransferases
Stephen Rea,Frank Eisenhaber,Dónal O'Carroll,Brian D. Strahl,Zu-Wen Sun,Manfred Schmid,Susanne Opravil,Karl Mechtler,Chris P. Ponting,C D Allis,Thomas Jenuwein +10 more
TL;DR: A functional interdependence of site-specific H3 tail modifications is revealed and a dynamic mechanism for the regulation of higher-order chromatin is suggested.