Open AccessRegulation of the Dot1 histone H3K79 methyltransferase by histone H4K16 acetylation
Author(s) -
Marco Igor ValenciaSánchez,
Pablo De Ioannes,
Miao Wang,
David M. Truong,
Rachel Lee,
JeanPaul Armache,
Jef D. Boeke,
KarimJean Armache
Publication year - 2021
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.abc6663
Subject(s) - histone methyltransferase , histone code , histone h2a , histone h1 , histone h3 , histone methylation , biology , histone h4 , histone octamer , histone , microbiology and biotechnology , biochemistry , gene expression , nucleosome , dna , gene , dna methylation
Cross-talk between histone modifications Histone modifications play pivotal roles within the intricate protein networks that underlie transcription and gene silencing in eukaryotic genomes. The enzymes that deposit them undergo spatiotemporal fine-tuning of their catalytic activity; one example is trans-histone cross-talk, in which one histone modification activates an enzyme responsible for another histone modification. Valencia-Sánchezet al. show that histone H4 lysine 16 acetylation (H4K16ac), a hallmark of decondensed, transcriptionally permissive chromatin, directly stimulates the Dot1 histone H3 lysine 79 methyltransferase. Structural, biochemical, and cellular data explain Dot1's regulation by H4K16ac and show how it coordinates with a second positive regulator of Dot1, histone H2B ubiquitination.Science , this issue p.eabc6663
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