Journal ArticleDOI
Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
Zu-Wen Sun,C. David Allis +1 more
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TLDR
It is shown that the ubiquitin-conjugating enzyme Rad6 (Ubc2) mediates methylation of histone H3 at lysine 4 (Lys 4) through ubiquitination of H2B at Lys 123 in yeast (Saccharomyces cerevisiae) to reveal a pathway leading to gene regulation through concerted histone modifications on distinct histone tails.Abstract:
In eukaryotes, the DNA of the genome is packaged with histone proteins to form nucleosomal filaments, which are, in turn, folded into a series of less well understood chromatin structures. Post-translational modifications of histone tail domains modulate chromatin structure and gene expression. Of these, histone ubiquitination is poorly understood. Here we show that the ubiquitin-conjugating enzyme Rad6 (Ubc2) mediates methylation of histone H3 at lysine 4 (Lys 4) through ubiquitination of H2B at Lys 123 in yeast (Saccharomyces cerevisiae). Moreover, H3 (Lys 4) methylation is abolished in the H2B-K123R mutant, whereas H3-K4R retains H2B (Lys 123) ubiquitination. These data indicate a unidirectional regulatory pathway in which ubiquitination of H2B (Lys 123) is a prerequisite for H3 (Lys 4) methylation. We also show that an H2B-K123R mutation perturbs silencing at the telomere, providing functional links between Rad6-mediated H2B (Lys 123) ubiquitination, Set1-mediated H3 (Lys 4) methylation, and transcriptional silencing. Thus, these data reveal a pathway leading to gene regulation through concerted histone modifications on distinct histone tails. We refer to this as 'trans-tail' regulation of histone modification, a stated prediction of the histone code hypothesis.read more
Citations
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Journal ArticleDOI
Dynamic Regulation of Histone H3 Methylated at Lysine 79 within a Tissue-specific Chromatin Domain
Hogune Im,Changwon Park,Qin Feng,Kirby D. Johnson,Carol M. Kiekhaefer,Kyunghee Choi,Yi Zhang,Emery H. Bresnick +7 more
TL;DR: It is found that H3-meK79 has a variable distribution within the murine β-globin locus in adult erythroid cells, being preferentially enriched at the active βmajor gene.
Journal ArticleDOI
The role of RAD6 in recombinational repair, checkpoints and meiosis via histone modification.
TL;DR: It is shown that RAD6 clearly plays a role in HRR in addition to its central role in PRR, and what is known about related repair pathways in other eukaryotes, including mammals is summarized.
Journal ArticleDOI
Altered nucleosome occupancy and histone H3K4 methylation in response to 'transcriptional stress'.
TL;DR: It is suggested that a ‘transcriptional stress’ signal sensed through Set1, Chd1, and possibly other factors, causes H3K4 hypermethylation of newly deposited nucleosomes at downstream positions within a gene.
Journal ArticleDOI
Human BRE1 is an E3 ubiquitin ligase for Ebp1 tumor suppressor.
Zhixue Liu,Sang Muk Oh,Masashi Okada,Xia Liu,Dongmei Cheng,Junmin Peng,Daniel J. Brat,Shi-Yong Sun,Wei Zhou,Wei Gu,Keqiang Ye +10 more
TL;DR: It is shown that hBre1 acts as an E3 ubiquitin ligase for Ebp1 tumor suppressor and promotes its polyubiquitination and degradation.
Book ChapterDOI
Histone ubiquitylation and the regulation of transcription.
TL;DR: Current research on the factors that regulate the attachment and removal of ubiquitin from histones are discussed, the relationship of histone ubiquitylation to histone methylation is described, and the roles of ubiquitylated histones in gene expression are focused on.
References
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Journal ArticleDOI
Translating the Histone Code
Thomas Jenuwein,C. David Allis +1 more
TL;DR: It is proposed that this epigenetic marking system represents a fundamental regulatory mechanism that has an impact on most, if not all, chromatin-templated processes, with far-reaching consequences for cell fate decisions and both normal and pathological development.
Journal ArticleDOI
The language of covalent histone modifications.
Brian D. Strahl,C D Allis +1 more
TL;DR: 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.
Journal ArticleDOI
Twenty-Five Years of the Nucleosome, Fundamental Particle of the Eukaryote Chromosome
Roger D. Kornberg,Yahli Lorch +1 more
TL;DR: The chromatin field needs much more information about structure beyond the nucleosome, and there is insufficient evidence that acetylation actually causes chromatin unfolding, and functional analysis in cell-free systems must be extended beyond theucleosome to the chromosomal context.
Journal ArticleDOI
Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails
Yi Zhang,Danny Reinberg +1 more
TL;DR: This work aims to demonstrate the efforts towards in-situ applicability of EMMARM, which aims to provide real-time information about the “building blocks” of EMT and its role in cancer progression.
Journal ArticleDOI
Histone acetylation and an epigenetic code
TL;DR: Recent evidence raises the interesting possibility that an acetylation-based code may operate through both mitosis and meiosis, providing a possible mechanism for germ-line transmission of epigenetic changes.