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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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ROS in cancer therapy: the bright side of the moon
Bruno Perillo,Marzia Di Donato,Antonio Pezone,Erika Di Zazzo,Pia Giovannelli,Giovanni Galasso,Gabriella Castoria,Antimo Migliaccio +7 more
TL;DR: The review will emphasize the molecular mechanisms useful for the development of therapeutic strategies that are based on modulating ROS levels to treat cancer, and report on the growing data that highlight the role of ROS generated by different metabolic pathways as Trojan horses to eliminate cancer cells.
Journal ArticleDOI
Multivalent engagement of chromatin modifications by linked binding modules.
TL;DR: It is proposed that multivalent interactions on a single histone tail and beyond may have a significant, if not dominant, role in chromatin transactions.
Journal ArticleDOI
Human PAD4 regulates histone arginine methylation levels via demethylimination.
Yanming Wang,Joanna Wysocka,Joyce Sayegh,Youngho Lee,Julie R. Perlin,Lauriebeth Leonelli,Lakshmi S. Sonbuchner,Charles H. McDonald,Richard G. Cook,Yali Dou,Robert G. Roeder,Steven Clarke,Michael R. Stallcup,C. David Allis,Scott A. Coonrod +14 more
TL;DR: It is demonstrated that human peptidylarginine deiminase 4 (PAD4) regulates histone Arg methylation by converting methyl-Arg to citrulline and releasing methylamine, and that PAD4 activity is linked with the transcriptional regulation of estrogen-responsive genes in MCF-7 cells.
Journal ArticleDOI
Structural Basis for the Methylation State-Specific Recognition of Histone H4-K20 by 53BP1 and Crb2 in DNA Repair
Maria Victoria Botuyan,Joseph Lee,Irene M. Ward,Ja Eun Kim,James R. Thompson,Junjie Chen,Georges Mer +6 more
TL;DR: This study reveals an evolutionarily conserved molecular mechanism of targeting DNA repair proteins to DSBs by direct recognition of H4-K20me2 through direct binding of 53BP1 and Crb2 to histone H4.
Journal ArticleDOI
The locus of evolution: evo devo and the genetics of adaptation
Hopi E. Hoekstra,Jerry A. Coyne +1 more
TL;DR: There is no theoretical or empirical basis for the evo devo contention that adaptations involving morphology evolve by genetic mechanisms different from those involving physiology and other traits, and substantial data on the genetic basis of adaptation from both genome-wide surveys and single-locus studies are examined.
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.