Journal ArticleDOI
The language of covalent histone modifications.
Brian D. Strahl,C D Allis +1 more
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TLDR
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.Abstract:
Histone proteins and the nucleosomes they form with DNA are the fundamental building blocks of eukaryotic chromatin. A diverse array of post-translational modifications that often occur on tail domains of these proteins has been well documented. Although the function of these highly conserved modifications has remained elusive, converging biochemical and genetic evidence suggests functions in several chromatin-based processes. We propose 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.read more
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An orally bioavailable chemical probe of the Lysine Methyltransferases EZH2 and EZH1.
Kyle D. Konze,Anqi Ma,Fengling Li,Dalia Barsyte-Lovejoy,Trevor Parton,Christopher J. MacNevin,Feng Liu,Cen Gao,Xi Ping Huang,Ekaterina Kuznetsova,Marie Rougie,Alice Jiang,Samantha G. Pattenden,Jacqueline L. Norris,Lindsey I. James,Bryan L. Roth,Peter Brown,Stephen V. Frye,Cheryl H. Arrowsmith,Klaus M. Hahn,Gang Greg Wang,Masoud Vedadi,Jian Jin +22 more
TL;DR: UNC1999 was the first orally bioavailable inhibitor that has high in vitro potency for wild-type and mutant EZH2 as well as EzH1, a closely related H3K27 methyltransferase that shares 96% sequence identity with EZh2 in their respective catalytic domains.
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NF-κB RelA Phosphorylation Regulates RelA Acetylation
Lin Feng Chen,Samuel A. Williams,Yajun Mu,Hiroyasu Nakano,James M. Duerr,Leonard Buckbinder,Warner C. Greene +6 more
TL;DR: Findings indicate that the acetylation of RelA at lysine 310 is importantly regulated by prior phosphorylation of serines 276 and 536, which indicates that phosphorylated and acetylated forms ofrelA display enhanced transcriptional activity.
Journal ArticleDOI
Histone H2A Monoubiquitination Represses Transcription by Inhibiting RNA Polymerase II Transcriptional Elongation
Wenlai Zhou,Ping Zhu,Jianxun Wang,Gabriel Pascual,Kenneth A. Ohgi,Jean Lozach,Christopher K. Glass,Michael G. Rosenfeld +7 more
TL;DR: The N-CoR/HDAC1/3 complex specifically recruits a specific histone H2A ubiquitin ligase, 2A-HUB/hRUL138, to a subset of regulated gene promoters, mediating a selective repression of a specific set of chemokine genes in macrophages.
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2-Deoxy-D-glucose reduces epilepsy progression by NRSF-CtBP–dependent metabolic regulation of chromatin structure
Mireia Garriga-Canut,Barry Schoenike,Romena Qazi,Karen Bergendahl,Timothy J Daley,Rebecca M Pfender,John F Morrison,Jeffrey C. Ockuly,Carl E. Stafstrom,Thomas P. Sutula,Avtar Roopra +10 more
TL;DR: 2DG potently reduces the progression of kindling and blocks seizure-induced increases in the expression of brain-derived neurotrophic factor and its receptor, TrkB, suggesting that anti-glycolytic compounds may represent a new class of drugs for treating epilepsy.
Journal ArticleDOI
Specificity of the HP1 chromo domain for the methylated N‐terminus of histone H3
Steven A. Jacobs,Steven A. Jacobs,Sean D. Taverna,Sean D. Taverna,Yinong Zhang,Scott D. Briggs,Jinmei Li,Joel C. Eissenberg,C. David Allis,Sepideh Khorasanizadeh +9 more
TL;DR: In situ immunofluorescence demonstrates that methyl‐K9 H3 and HP1 co‐localize to the heterochromatic regions of Drosophila polytene chromosomes and indicates that sequence diversity in chromo domains may lead to diverse functions in eukaryotic gene regulation.
References
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Journal ArticleDOI
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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Histone acetylation in chromatin structure and transcription
TL;DR: The amino termini of histones extend from the nucleosomal core and are modified by acetyltransferases and deacetylases during the cell cycle, which may direct histone assembly and help regulate the unfolding and activity of genes.
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Protein modules and signalling networks
TL;DR: This work highlights conserved protein domains that act as key regulatory participants in many of these different signalling pathways in multicellular organisms.
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Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation.
Michael J. Hendzel,Y Wei,Michael A. Mancini,A. Van Hooser,Tamara A. Ranalli,Bill R. Brinkley,David P. Bazett-Jones,C D Allis +7 more
TL;DR: It is proposed that the singular phosphorylation of the amino-terminus of histone H3 may be involved in facilitating two key functions during mitosis: (1) regulate protein-protein interactions to promote binding of trans-acting factors that “drive” chromatin condensation as cells enter M-phase and (2) coordinate chromatin decondensation associated with M- phase.
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Histone acetylation and transcriptional regulatory mechanisms
TL;DR: Understanding of the causal relationship between histone acetylation and gene expression has been enhanced dramatically by the identification of proteins with intrinsic hist one acetylase and deacetylase activity, which led to a major paradigm shift in understanding of chromatin structure and transcription regulation.