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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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Posttranslationale Proteinmodifikation: die Chemie der Proteomdiversifizierung

TL;DR: The posttranslationale modifikationen (e.g., Phosphory, Acetylierung, Glycosy, Methylierung and Ubiquitinierung) are gerichtete post translationalen Modifikations as mentioned in this paper.
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Reading, writing and editing methylated lysines on histone tails: new insights from recent structural studies.

TL;DR: Recent advances in the structural description of the reading, writing, and editing of two histone methylation marks with opposite functions are reviewed: at histone H3 lysine 4 (H3K4)-associated with actively transcribed genes, and at H3K27-a hallmark of silenced chromatin.
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SPR-5 is a histone H3K4 demethylase with a role in meiotic double-strand break repair.

TL;DR: This work reports a unique role for the Caenorhabditis elegans histone demethylase SPR-5 in meiotic DNA double-strand break repair (DSBR), and shows a rapid subcellular relocalization upon DSB-inducing treatment, which suggests that SPR- 5 may function directly in DSBR.
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Epigenetics, Development, and the Kidney

TL;DR: DNA-binding factors such as Pax2/8, which are essential for the intermediate mesoderm and the renal epithelial lineage, could provide the locus and tissue specificity for histone methylation and chromatin remodeling and thus establish a kidney-specific fate.
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Role of Histone-Modifying Enzymes and Their Complexes in Regulation of Chromatin Biology

TL;DR: This model provides a simple but conceptually accurate model for the biological role of histone post-translational modifications (PTMs) and the structure of nucleosomes, their natural substrate, will be described.
References
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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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