G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis (Q24673923): Difference between revisions

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Kenji Sugimoto

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Masami Nozaki

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Jun Ueda

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Tsutomu Ohta

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Misao Ohki

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Mikiko Fukuda

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Naoki Takeda

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Hiroyuki Niida

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Hiroyuki Kato

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Yoichi Shinkai

original language of film or TV show

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English

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publication date

15 July 2002

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published in

Genes & Development

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volume

16

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issue

14

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page(s)

1779-91

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cites work

A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells

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SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins

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Involvement of a novel zinc finger protein, MIZF, in transcriptional repression by interacting with a methyl-CpG-binding protein, MBD2

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Transcriptional repression by the retinoblastoma protein through the recruitment of a histone methyltransferase

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Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1

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Isolation and characterization of Suv39h2, a second histone H3 methyltransferase gene that displays testis-specific expression

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Regulation of chromatin structure by site-specific histone H3 methyltransferases

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Set domain-dependent regulation of transcriptional silencing and growth control by SUV39H1, a mammalian ortholog of Drosophila Su(var)3-9

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Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31

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The G9a gene in the human major histocompatibility complex encodes a novel protein containing ankyrin-like repeats

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Translating the Histone Code

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

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Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins

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The language of covalent histone modifications

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Histone acetylation in chromatin structure and transcription

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Molecular cloning of ESET, a novel histone H3-specific methyltransferase that interacts with ERG transcription factor

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