scholarly journals Chromatin Binding of SRp20 and ASF/SF2 and Dissociation from Mitotic Chromosomes Is Modulated by Histone H3 Serine 10 Phosphorylation

2009 ◽  
Vol 33 (4) ◽  
pp. 450-461 ◽  
Author(s):  
Rebecca J. Loomis ◽  
Yoshinori Naoe ◽  
J. Brandon Parker ◽  
Velibor Savic ◽  
Matthew R. Bozovsky ◽  
...  
Keyword(s):  
Histone H3 ◽  
Chromatin Binding ◽  
Mitotic Chromosomes

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.

scholarly journals Phosphorylation of Histone H3 at Serine 10 Cannot Account Directly for the Detachment of Human Heterochromatin Protein 1γ from Mitotic Chromosomes in Plant Cells

2002 ◽  
Vol 277 (34) ◽  
pp. 30921-30927 ◽  
Author(s):  
Ephraim Fass ◽  
Shai Shahar ◽  
Jing Zhao ◽  
Assaf Zemach ◽  
Yigal Avivi ◽  
...  
Keyword(s):  
Histone H3 ◽  
Plant Cells ◽  
Mitotic Chromosomes ◽  
Heterochromatin Protein

scholarly journals Cell Cycle-dependent Expression and Nucleolar Localization of hCAP-H

2001 ◽  
Vol 12 (11) ◽  
pp. 3527-3537 ◽  
Author(s):  
Olga A. Cabello ◽  
Elena Eliseeva ◽  
WeiGong He ◽  
Hagop Youssoufian ◽  
Sharon E. Plon ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Histone H3 ◽  
Chromosome Condensation ◽  
Nucleolar Localization ◽  
Mitotic Chromosomes ◽  
Proliferating Cells ◽  
Protein Levels ◽  
Sister Chromatids ◽  
H3 Phosphorylation ◽  
Histone H3 Phosphorylation

Condensin is a conserved 13S heteropentamer composed of two nonidentical structural maintenance of chromosome (SMC) family proteins, in Xenopus XCAP-C and XCAP-E, and three regulatory subunits, XCAP-D2, XCAP-G, and XCAP-H. Both biochemical and genetic analyses have demonstrated an essential role for the 13S condensin complex in mitotic chromosome condensation. Further, a potential requirement for condensin in completion of chromatid arm separation in early anaphase is demonstrated by the mutational phenotypes of the Drosophila homologues ofXCAP-H, barren and XCAP-C,DmSMC4. In this study we have investigated the expression and subcellular distribution of hCAP-H, the human homolog of XCAP-H, in order to better understand its cellular functions. Transcription of hCAP-H was restricted to proliferating cells with highest expression during the G2 phase of the cell cycle. In contrast, cellular hCAP-H protein levels were constant throughout the cell cycle. hCAP-H was found to be associated with mitotic chromosomes exhibiting a nonuniform but symmetric distribution along sister chromatids. The symmetry of hCAP-H association with sister chromatids suggests that there are sequence-dependent domains of condensin aggregation. During interphase hCAP-H, -C, and -E, have distinct punctate nucleolar localization, suggesting that condensin may associate with and modulate the conformation and function of rDNA. hCAP-H association with condensed chromatin was not observed in the early phase of chromosome condensation when histone H3 phosphorylation has already taken place. This finding is consistent with the hypothesis that histone H3 phosphorylation precedes condensin-mediated condensation.

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 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 A Bromodomain Protein, MCAP, Associates with Mitotic Chromosomes and Affects G2-to-M Transition

2000 ◽  
Vol 20 (17) ◽  
pp. 6537-6549 ◽  
Author(s):  
Anup Dey ◽  
Jan Ellenberg ◽  
Andrea Farina ◽  
Allen E. Coleman ◽  
Tetsuo Maruyama ◽  
...  
Keyword(s):  
Mitotic Chromosome ◽  
Histone H3 ◽  
Growth Stimulation ◽  
Nuclear Factor ◽  
Cell Nuclei ◽  
Mitotic Chromosomes ◽  
H3 Phosphorylation ◽  
Chromosomal Condensation ◽  
Histone H3 Phosphorylation ◽  
Exquisite Specificity

ABSTRACT We describe a novel nuclear factor called mitotic chromosome-associated protein (MCAP), which belongs to the poorly understood BET subgroup of the bromodomain superfamily. Expression of the 200-kDa MCAP was linked to cell division, as it was induced by growth stimulation and repressed by growth inhibition. The most notable feature of MCAP was its association with chromosomes during mitosis, observed at a time when the majority of nuclear regulatory factors were released into the cytoplasm, coinciding with global cessation of transcription. Indicative of its predominant interaction with euchromatin, MCAP localized on mitotic chromosomes with exquisite specificity: (i) MCAP-chromosome association became evident subsequent to the initiation of histone H3 phosphorylation and early chromosomal condensation; and (ii) MCAP was absent from centromeres, the sites of heterochromatin. Supporting a role for MCAP in G2/M transition, microinjection of anti-MCAP antibody into HeLa cell nuclei completely inhibited the entry into mitosis, without abrogating the ongoing DNA replication. These results suggest that MCAP plays a role in a process governing chromosomal dynamics during mitosis.

scholarly journals A phospho/methyl switch at histone H3 regulates TFIID association with mitotic chromosomes

2010 ◽  
Vol 29 (23) ◽  
pp. 3967-3978 ◽  
Author(s):  
Radhika A Varier ◽  
Nikolay S Outchkourov ◽  
Petra de Graaf ◽  
Frederik M A van Schaik ◽  
Henk Jan L Ensing ◽  
...  
Keyword(s):  
Histone H3 ◽  
Mitotic Chromosomes

scholarly journals Phosphorylation Regulates Binding of the Human Papillomavirus Type 8 E2 Protein to Host Chromosomes

2012 ◽  
Vol 86 (18) ◽  
pp. 10047-10058 ◽  
Author(s):  
Vandana Sekhar ◽  
Alison A. McBride
Keyword(s):  
Human Papillomavirus ◽  
Posttranslational Modifications ◽  
S Phase ◽  
Chromatin Binding ◽  
Genome Maintenance ◽  
Mitotic Chromosomes ◽  
E2 Protein ◽  
Viral Genomes ◽  
Daughter Cells ◽  
Host Nucleus

The papillomavirus E2 proteins are indispensable for the viral life cycle, and their functions are subject to tight regulation. The E2 proteins undergo posttranslational modifications that regulate their properties and roles in viral transcription, replication, and genome maintenance. During persistent infection, the E2 proteins from many papillomaviruses act as molecular bridges that tether the viral genomes to host chromosomes to retain them within the host nucleus and to partition them to daughter cells. The betapapillomavirus E2 proteins bind to pericentromeric regions of host mitotic chromosomes, including the ribosomal DNA loci. We recently reported that two residues (arginine 250 and serine 253) within the chromosome binding region of the human papillomavirus type 8 (HPV8) E2 protein are required for this binding. In this study, we show that serine 253 is phosphorylated, most likely by protein kinase A, and this modulates the interaction of the E2 protein with cellular chromatin. Furthermore, we show that this phosphorylation occurs in S phase, increases the half-life of the E2 protein, and promotes chromatin binding from S phase through mitosis.

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.

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