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Histone demethylation mediated by the nuclear amine oxidase homolog lsd1

Yang Shi, +1 more
- 16 Dec 2005 - 
- Vol. 119, Iss: 7, pp 941-953
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.
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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.

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Citations
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HISTONE DEACETYLASE19 interacts with HSL1 and participates in the repression of seed maturation genes in Arabidopsis seedlings.

TL;DR: It is found that mutations in HDA19 resulted in the ectopic expression of seed maturation genes in seedlings, which was associated with increased levels of gene activation marks, but decreased levels of the gene repression mark Histone H3 Lys 27 tri-methylation (H3K27me3) in the promoter and/or coding regions.
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Histone modifying enzymes and cancer: going beyond histones

TL;DR: It is proposed that multiple protein modifications, including phosphorylation, methylation, and acetylation, cross regulate one another to coordinate intermolecular signaling, and that miscues in this regulation can lead to oncogenesis.
Journal ArticleDOI

Mechanisms of human histone and nucleic acid demethylases

TL;DR: The discovery that protein and nucleic acid demethylation is common opens up the possibility of 'methylation cycles' of functional importance, including in the regulation of gene expression, as well as chemically viable mechanisms for biological dem methylation.
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The small glycine-rich RNA binding protein AtGRP7 promotes floral transition in Arabidopsis thaliana

TL;DR: In this article, the authors identify a role for AtGRP7 as a flowering-time gene in Arabidopsis thaliana, and they show that atgrp7-1 T-DNA mutant flowers later than wild-type plants under both long and short days.
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Structure and function of histone methylation binding proteins

TL;DR: This review summarizes current knowledge of the structures and modes of recognition employed by the PHD, Tudor, and MBT domains in their interactions with target histone peptides.
References
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Journal ArticleDOI

Translating the Histone Code

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

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.
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Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain.

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.
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Regulation of chromatin structure by site-specific histone H3 methyltransferases

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.
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