scholarly journals KDM3A-mediated demethylation of histone H3 lysine 9 facilitates the chromatin binding of Neurog2 during neurogenesis

Development ◽  
2017 ◽  
Vol 144 (20) ◽  
pp. 3674-3685 ◽  
Author(s):  
Hao Lin ◽  
Xuechen Zhu ◽  
Geng Chen ◽  
Lei Song ◽  
Li Gao ◽  
...  
Keyword(s):  
Histone H3 ◽  
Chromatin Binding

scholarly journals The Trithorax group protein ASH1 requires a combination of BAH domain and AT hooks, but not the SET domain, for mitotic chromatin binding and survival

Chromosoma ◽  
2021 ◽  
Author(s):  
Philipp A. Steffen ◽  
Christina Altmutter ◽  
Eva Dworschak ◽  
Sini Junttila ◽  
Attila Gyenesei ◽  
...  
Keyword(s):  
Transcriptional Profiling ◽  
Histone H3 ◽  
Chromatin Binding ◽  
Set Domain ◽  
Trithorax Group ◽  
Trxg Protein ◽  
Group Protein ◽  
Bah Domain ◽  
Mitotic Chromatin

AbstractThe Drosophila Trithorax group (TrxG) protein ASH1 remains associated with mitotic chromatin through mechanisms that are poorly understood. ASH1 dimethylates histone H3 at lysine 36 via its SET domain. Here, we identify domains of the TrxG protein ASH1 that are required for mitotic chromatin attachment in living Drosophila. Quantitative live imaging demonstrates that ASH1 requires AT hooks and the BAH domain but not the SET domain for full chromatin binding in metaphase, and that none of these domains are essential for interphase binding. Genetic experiments show that disruptions of the AT hooks and the BAH domain together, but not deletion of the SET domain alone, are lethal. Transcriptional profiling demonstrates that intact ASH1 AT hooks and the BAH domain are required to maintain expression levels of a specific set of genes, including several involved in cell identity and survival. This study identifies in vivo roles for specific ASH1 domains in mitotic binding, gene regulation, and survival that are distinct from its functions as a histone methyltransferase.

Regulation of HP1–chromatin binding by histone H3 methylation and phosphorylation

Nature ◽  
2005 ◽  
Vol 438 (7071) ◽  
pp. 1116-1122 ◽  
Author(s):  
Wolfgang Fischle ◽  
Boo Shan Tseng ◽  
Holger L. Dormann ◽  
Beatrix M. Ueberheide ◽  
Benjamin A. Garcia ◽  
...  
Keyword(s):  
Histone H3 ◽  
Chromatin Binding ◽  
Histone H3 Methylation

scholarly journals RBBP4 modulates gene activity through acetylation and methylation of histone H3 lysine 27

2021 ◽  
Author(s):  
Weipeng Mu ◽  
Noel S Murcia ◽  
Keriayn N. Smith ◽  
Debashish U Menon ◽  
Della Yee ◽  
...  
Keyword(s):  
Histone H3 ◽  
Embryonic Stem ◽  
Mouse Embryonic Stem Cell ◽  
Regulatory Elements ◽  
Chromatin Binding ◽  
Disease Treatment ◽  
Polycomb Repressive Complex 2 ◽  
H3k27 Methylation ◽  
Transcriptional Changes ◽  
Stem Cell Lines

AbstractRBBP4 is a core subunit of polycomb repressive complex 2 (PRC2) and HDAC1/2-containing complexes, which are responsible for histone H3 lysine 27 (H3K27) methylation and deacetylation respectively. However, the mechanisms by which RBBP4 modulates the functions of these complexes remain largely unknown. We generated viable mouse embryonic stem cell lines with RBBP4 mutations that disturbed methylation and acetylation of H3K27 on target chromatin and found that RBBP4 is required for PRC2 assembly and H3K27me3 establishment on target chromatin. Moreover, in the absence of EED and SUZ12, RBBP4 maintained chromatin binding on PRC2 loci, suggesting that the pre-existence of RBBP4 on nucleosomes serves to recruit PRC2 to restore H3K27me3 on newly synthesized histones. As such, disruption of RBBP4 function led to dramatic changes in transcriptional profiles. In spite of the PRC2 association, we found that transcriptional changes were more closely tied to the deregulation of H3K27ac rather than H3K27me3 where increased levels of H3K27ac were found on numerous cis-regulatory elements, especially putative enhancers. These data suggest that RBBP4 controls acetylation levels by adjusting the activity of HDAC complexes. As histone methylation and acetylation have been implicated in cancer and neural disease, RBBP4 could serve as a potential target for disease treatment.

scholarly journals How HP1 Post-Translational Modifications Regulate Heterochromatin Formation and Maintenance

Cells ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 1460
Author(s):  
Raquel Sales-Gil ◽  
Paola Vagnarelli
Keyword(s):  
Recent Literature ◽  
Histone H3 ◽  
Chromatin Binding ◽  
Heterochromatin Protein 1 ◽  
Binding Ability ◽  
Heterochromatin Protein ◽  
Post Translational Modifications ◽  
Heterochromatin Formation

Heterochromatin Protein 1 (HP1) is a highly conserved protein that has been used as a classic marker for heterochromatin. HP1 binds to di- and tri-methylated histone H3K9 and regulates heterochromatin formation, functions and structure. Besides the well-established phosphorylation of histone H3 Ser10 that has been shown to modulate HP1 binding to chromatin, several studies have recently highlighted the importance of HP1 post-translational modifications and additional epigenetic features for the modulation of HP1-chromatin binding ability and heterochromatin formation. In this review, we summarize the recent literature of HP1 post-translational modifications that have contributed to understand how heterochromatin is formed, regulated and maintained.

scholarly journals NuA3 HAT antagonizes the Rpd3S and Rpd3L HDACs to optimize mRNA and lncRNA expression dynamics

2020 ◽  
Vol 48 (19) ◽  
pp. 10753-10767
Author(s):  
Ji Hyun Kim ◽  
Chae Young Yoon ◽  
Yukyung Jun ◽  
Bo Bae Lee ◽  
Ji Eun Lee ◽  
...  
Keyword(s):  
Transcriptional Repression ◽  
Histone Deacetylases ◽  
Binding Proteins ◽  
Histone Acetyltransferase ◽  
Histone H3 ◽  
Terminal Region ◽  
Chromatin Binding ◽  
Phd Finger ◽  
Lncrna Expression ◽  
Plant Homeodomain

Abstract In yeast, NuA3 histone acetyltransferase (NuA3 HAT) promotes acetylation of histone H3 lysine 14 (H3K14) and transcription of a subset of genes through interaction between the Yng1 plant homeodomain (PHD) finger and H3K4me3. Although NuA3 HAT has multiple chromatin binding modules with distinct specificities, their interdependence and combinatorial actions in chromatin binding and transcription remain unknown. Modified peptide pulldown assays reveal that the Yng1 N-terminal region is important for the integrity of NuA3 HAT by mediating the interaction between core subunits and two methyl-binding proteins, Yng1 and Pdp3. We further uncover that NuA3 HAT contributes to the regulation of mRNA and lncRNA expression dynamics by antagonizing the histone deacetylases (HDACs) Rpd3S and Rpd3L. The Yng1 N-terminal region, the Nto1 PHD finger and Pdp3 are important for optimal induction of mRNA and lncRNA transcription repressed by the Set2-Rpd3S HDAC pathway, whereas the Yng1 PHD finger–H3K4me3 interaction affects transcriptional repression memory regulated by Rpd3L HDAC. These findings suggest that NuA3 HAT uses distinct chromatin readers to compete with two Rpd3-containing HDACs to optimize mRNA and lncRNA expression dynamics.

scholarly journals PRC2 activates interferon-stimulated genes indirectly by repressing miRNAs in glioblastoma

2019 ◽  
Author(s):  
Haridha Shivram ◽  
Steven V. Le ◽  
Vishwanath R. Iyer
Keyword(s):  
Gene Expression ◽  
Cell Lines ◽  
Anaplastic Astrocytoma ◽  
Gene Expression Analysis ◽  
Histone H3 ◽  
Chromatin Binding ◽  
Chromosome 14 ◽  
Methyltransferase Activity ◽  
Polycomb Repressive Complex 2 ◽  
Interferon Stimulated Genes

AbstractPolycomb repressive complex 2 (PRC2) is a chromatin binding complex that represses gene expression by methylating histone H3 at K27 to establish repressed chromatin domains. PRC2 can either regulate genes directly through the methyltransferase activity of its component EZH2 or indirectly by regulating other gene regulators. Gene expression analysis of glioblastoma (GBM) cells lacking EZH2 showed that PRC2 regulates hundreds of interferon-stimulated genes (ISGs). We found that PRC2 directly represses several ISGs and also indirectly activates a distinct set of ISGs. Assessment of EZH2 binding proximal to miRNAs showed that PRC2 directly represses miRNAs encoded in the chromosome 14 imprinted DLK1-DIO3 locus. We found that repression of this locus by PRC2 occurs in immortalized GBM-derived cell lines as well as in primary bulk tumors from GBM and anaplastic astrocytoma patients. Through repression of these miRNAs and several other miRNAs, PRC2 activates a set of ISGs that are targeted by these miRNAs. This PRC2-miRNA-ISG network is likely to be important in regulating gene expression programs in GBM.

scholarly journals DOT1L suppresses nuclear RNAi originating from enhancer elements in Caenorhabditis elegans

2018 ◽  
Author(s):  
Ruben Esse ◽  
Ekaterina Gushchanskaia ◽  
Avery Lord ◽  
Alla Grishok
Keyword(s):  
Caenorhabditis Elegans ◽  
Neural Activity ◽  
Target Genes ◽  
Histone H3 ◽  
Chromatin Binding ◽  
Lower Efficiency ◽  
Double Stranded Rna ◽  
Bidirectional Transcription ◽  
Underlying Mechanisms ◽  
Nuclear Rnai

ABSTRACTMethylation of histone H3 on lysine 79 (H3K79) by DOT1L is associated with actively transcribed genes. Earlier, we described that DOT-1.1, the Caenorhabditis elegans DOT1L homologue, cooperates with the chromatin-binding protein ZFP-1 (AF10 homologue) to negatively modulate transcription of highly and widely expressed target genes. Also, reduction in ZFP-1 levels has long been associated with lower efficiency of RNA interference (RNAi) triggered by exogenous double-stranded RNA (dsRNA), but the reason for this is not clear. Here, we demonstrate that DOT1L suppresses bidirectional transcription, including that producing enhancer RNAs, thereby preventing dsRNA formation and ectopic RNAi. This ectopic elevation of endogenous dsRNA may engage the Dicer complex and, therefore, limit efficiency of exogenous RNAi. Our insight provides a novel perspective on the underlying mechanisms of DOT1L function in development, neural activity, and cancer.

scholarly journals In vivo dissection of the chromosome condensation machinery

2002 ◽  
Vol 156 (5) ◽  
pp. 805-815 ◽  
Author(s):  
Brigitte D. Lavoie ◽  
Eileen Hogan ◽  
Douglas Koshland
Keyword(s):  
Topoisomerase Ii ◽  
Mitotic Chromosome ◽  
Chromosome Structure ◽  
Histone H3 ◽  
Chromosome Condensation ◽  
Chromatin Binding ◽  
Condensin Complex ◽  
Topo Ii ◽  
Structural Maintenance Of Chromosome

The machinery mediating chromosome condensation is poorly understood. To begin to dissect the in vivo function(s) of individual components, we monitored mitotic chromosome structure in mutants of condensin, cohesin, histone H3, and topoisomerase II (topo II). In budding yeast, both condensation establishment and maintenance require all of the condensin subunits, but not topo II activity or phospho-histone H3. Structural maintenance of chromosome (SMC) protein 2, as well as each of the three non-SMC proteins (Ycg1p, Ycs4p, and Brn1p), was required for chromatin binding of the condensin complex in vivo. Using reversible condensin alleles, we show that chromosome condensation does not involve an irreversible modification of condensin or chromosomes. Finally, we provide the first evidence of a mechanistic link between condensin and cohesin function. A model discussing the functional interplay between cohesin and condensin is presented.

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