PR-Set7 Is a Nucleosome-Specific Methyltransferase that Modifies Lysine 20 of Histone H4 and Is Associated with Silent Chromatin
Kenichi Nishioka,Judd C. Rice,Kavitha Sarma,Hediye Erdjument-Bromage,Janis Werner,Yanming Wang,Sergei Chuikov,Pablo Valenzuela,Paul Tempst,Ruth Steward,John T. Lis,C. David Allis,Danny Reinberg +12 more
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TLDR
The hypothesis that methylation of H4 lysine 20 maintains silent chromatin, in part, by precluding neighboring acetylation on the H4 tail is supported.About:
This article is published in Molecular Cell.The article was published on 2002-06-01 and is currently open access. It has received 555 citations till now. The article focuses on the topics: Histone methyltransferase & Histone H4.read more
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Histone demethylation mediated by the nuclear amine oxidase homolog lsd1
Yang Shi,Yujiang Shi +1 more
TL;DR: 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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The diverse functions of histone lysine methylation.
Cyrus Martin,Yi Zhang +1 more
TL;DR: Recent advances in understanding of how lysine methylation functions in these diverse biological processes are summarized, and questions that need to be addressed in the future are raised.
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Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer
Mario F. Fraga,Esteban Ballestar,Ana Villar-Garea,Manuel Boix-Chornet,Jesús Espada,Gunnar Schotta,Tiziana Bonaldi,Claire E. Haydon,Santiago Ropero,Kevin Petrie,N. Gopalakrishna Iyer,Alberto Pérez-Rosado,Enrique Calvo,Juan Antonio López,Amparo Cano,María José Calasanz,Dolors Colomer,Miguel A. Piris,Natalie G. Ahn,Natalie G. Ahn,Axel Imhof,Carlos Caldas,Thomas Jenuwein,Manel Esteller +23 more
TL;DR: It is found that cancer cells had a loss of monoacetylated and trimethylated forms of histone H4 early and accumulated during the tumorigenic process, which is a common hallmark of human tumor cells.
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Histone methylation: a dynamic mark in health, disease and inheritance
Eric L. Greer,Yang Shi +1 more
TL;DR: This work provides a broad overview of how histone methylation is regulated and leads to biological outcomes and suggests its links to disease and ageing and possibly to transmission of traits across generations are illustrated.
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Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein
TL;DR: The isolation of a multiprotein E(z) complex that contains extra sex combs, suppressor of zeste-12, and the histone binding proteins RbAp46/RbAp48 is reported, which possesses HMT activity with specificity for Lys 9 (K9) and Lys 27 (K27) of histone H3.
References
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G Köhler,C. Milstein +1 more
TL;DR: The derivation of a number of tissue culture cell lines which secrete anti-sheep red blood cell (SRBC) antibodies is described here, made by fusion of a mouse myeloma and mouse spleen cells from an immunised donor.
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TL;DR: It is proposed that distinct histone modifications, on one or more tails, act sequentially or in combination to form a ‘histone code’ that is, read by other proteins to bring about distinct downstream events.
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Crystal structure of the nucleosome core particle at 2.8 Å resolution
TL;DR: The X-ray crystal structure of the nucleosome core particle of chromatin shows in atomic detail how the histone protein octamer is assembled and how 146 base pairs of DNA are organized into a superhelix around it.
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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.
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Role of Histone H3 Lysine 9 Methylation in Epigenetic Control of Heterochromatin Assembly
TL;DR: In vivo evidence is provided that lysine 9 of histone H3 (H3 Lys9) is preferentially methylated by the Clr4 protein at heterochromatin-associated regions in fission yeast, defining a conserved pathway wherein sequential histone modifications establish a “histone code” essential for the epigenetic inheritance of heterochROMatin assembly.