Journal ArticleDOI
The language of covalent histone modifications.
Brian D. Strahl,C D Allis +1 more
Reads0
Chats0
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
Citations
More filters
Journal ArticleDOI
Conversion of cysteine into dehydroalanine enables access to synthetic histones bearing diverse post-translational modifications.
TL;DR: The precision of chemical synthesis is presently unrivaled in accessing purified histones with multiple PTMs, which may be especially valuable when the associated modifying enzyme or co-substrates are unknown or hard to acquire.
Journal ArticleDOI
Targeted recruitment of a histone H4-specific methyltransferase by the transcription factor YY1
Natalie Rezai-Zadeh,Xiaohong Zhang,Fares Namour,György Fejer,Yu-Der Wen,Ya-Li Yao,Ildiko Györy,Kenneth P. Wright,Edward Seto +8 more
TL;DR: The sequence-specific DNA-binding transcription factor Yin Yang 1 (YY1) binds to and recruits the histone H4 (Arg 3)-specific methyltransferase, PRMT1, to a YY1-activated promoter and provides one mechanism by which HMTs can be recruited to chromatin to activate gene expression.
Journal ArticleDOI
A Peek into the Complex Realm of Histone Phosphorylation
TL;DR: In this article, the authors extensively review published information on the complexities of histone phosphorylation, the roles of proteins recognizing these modifications and the resuting physiological outcome, and importantly, future challenges and opportunities in this fast-moving field.
Journal ArticleDOI
Two-pronged Binding with Bromodomain-containing Protein 4 Liberates Positive Transcription Elongation Factor b from Inactive Ribonucleoprotein Complexes
Sebastian Schröder,Sungyoo Cho,Lei Zeng,Qiang Zhang,Katrin Kaehlcke,Lily Mak,Joann Lau,Dwayne Bisgrove,Martina Schnölzer,Eric Verdin,Ming-Ming Zhou,Melanie Ott +11 more
TL;DR: A model where two BRD4 domains, the second bromodomain and the PID, bind P-TEFb and are required for full transcriptional activation of P- TEFb response genes is supported.
Journal ArticleDOI
BUR Kinase Selectively Regulates H3 K4 Trimethylation and H2B Ubiquitylation through Recruitment of the PAF Elongation Complex
R. Nicholas Laribee,Nevan J. Krogan,Tiaojiang Xiao,Yoichiro Shibata,Timothy P. Hughes,Jack Greenblatt,Brian D. Strahl +6 more
TL;DR: The data reveal a novel function for the Bur1/2 kinase in transcriptional regulation through the selective control of histone modifications and suggest that BUR acts upstream of these factors to control their function.
References
More filters
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.
Journal ArticleDOI
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.
Journal ArticleDOI
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.
Journal ArticleDOI
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.
Journal ArticleDOI
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.