Faculty Opinions recommendation of Accurate Recycling of Parental Histones Reproduces the Histone Modification Landscape during DNA Replication.

2018 ◽  
Author(s):  
Judith Zaugg
Keyword(s):  
Dna Replication ◽  
Histone Modification

scholarly journals Histone H3 Lysine 4 Methylation Marks Postreplicative Human Cytomegalovirus Chromatin

2012 ◽  
Vol 86 (18) ◽  
pp. 9817-9827 ◽  
Author(s):  
Alexandra Nitzsche ◽  
Charlotte Steinhäußer ◽  
Katrin Mücke ◽  
Christina Paulus ◽  
Michael Nevels
Keyword(s):  
Dna Replication ◽  
Dna Synthesis ◽  
Histone Modification ◽  
Dna Polymerase ◽  
Human Cytomegalovirus ◽  
Viral Genome ◽  
Histone H3 ◽  
Viral Dna ◽  
The Impact ◽  
Preferential Incorporation

In the nuclei of permissive cells, human cytomegalovirus genomes form nucleosomal structures initially resembling heterochromatin but gradually switching to a euchromatin-like state. This switch is characterized by a decrease in histone H3 K9 methylation and a marked increase in H3 tail acetylation and H3 K4 methylation across the viral genome. We used ganciclovir and a mutant virus encoding a reversibly destabilized DNA polymerase to examine the impact of DNA replication on histone modification dynamics at the viral chromatin. The changes in H3 tail acetylation and H3 K9 methylation proceeded in a DNA replication-independent fashion. In contrast, the increase in H3 K4 methylation proved to depend widely on viral DNA synthesis. Consistently, labeling of nascent DNA using “click chemistry” revealed preferential incorporation of methylated H3 K4 into viral (but not cellular) chromatin during or following DNA replication. This study demonstrates largely selective epigenetic tagging of postreplicative human cytomegalovirus chromatin.

scholarly journals Accurate Recycling of Parental Histones Reproduces the Histone Modification Landscape during DNA Replication

2018 ◽  
Vol 72 (2) ◽  
pp. 239-249.e5 ◽  
Author(s):  
Nazaret Reverón-Gómez ◽  
Cristina González-Aguilera ◽  
Kathleen R. Stewart-Morgan ◽  
Nataliya Petryk ◽  
Valentin Flury ◽  
...  
Keyword(s):  
Dna Replication ◽  
Histone Modification

scholarly journals Dynamics of SAS-I mediated H4 K16 acetylation during DNA replication in yeast

PLoS ONE ◽  
2021 ◽  
Vol 16 (5) ◽  
pp. e0251660
Author(s):  
Mark Boltengagen ◽  
Anke Samel-Pommerencke ◽  
David Fechtig ◽  
Ann E. Ehrenhofer-Murray
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Dna Replication ◽  
Gene Silencing ◽  
Histone Modification ◽  
Replication Fork ◽  
Growth Defect ◽  
Cellular Functions ◽  
Genome Wide ◽  
Sir Complex ◽  
Subtelomeric Regions

The acetylation of H4 lysine 16 (H4 K16Ac) in Saccharomyces cerevisiae counteracts the binding of the heterochromatin complex SIR to chromatin and inhibits gene silencing. Contrary to other histone acetylation marks, the H4 K16Ac level is high on genes with low transcription, whereas highly transcribed genes show low H4 K16Ac. Approximately 60% of cellular H4 K16Ac in S. cerevisiae is provided by the SAS-I complex, which consists of the MYST-family acetyltransferase Sas2, Sas4 and Sas5. The absence of SAS-I causes inappropriate spreading of the SIR complex and gene silencing in subtelomeric regions. Here, we investigated the genome-wide dynamics of SAS-I dependent H4 K16Ac during DNA replication. Replication is highly disruptive to chromatin and histone marks, since histones are removed to allow progression of the replication fork, and chromatin is reformed with old and new histones after fork passage. We found that H4 K16Ac appears in chromatin immediately upon replication. Importantly, this increase depends on the presence of functional SAS-I complex. Moreover, the appearance of H4 K16Ac is delayed in genes that are strongly transcribed. This indicates that transcription counteracts SAS-I-mediated H4 K16 acetylation, thus “sculpting” histone modification marks at the time of replication. We furthermore investigated which acetyltransferase acts redundantly with SAS-I to acetylate H4 K16Ac. esa1Δ sds3Δ cells, which were also sas2Δ sir3Δ in order to maintain viability, contained no detectable H4 K16Ac, showing that Esa1 and Sas2 are redundant for cellular H4 K16 acetylation. Furthermore, esa1Δ sds3Δ sas2Δ sir3Δ showed a more pronounced growth defect compared to the already defective esa1Δ sds3Δ sir3Δ. This indicates that SAS-I has cellular functions beyond preventing the spreading of heterochromatin.

scholarly journals Holding on through DNA Replication: Histone Modification or Modifier?

Cell ◽  
2012 ◽  
Vol 150 (5) ◽  
pp. 875-877 ◽  
Author(s):  
Susan M. Abmayr ◽  
Jerry L. Workman
Keyword(s):  
Dna Replication ◽  
Histone Modification

scholarly journals The p55 subunit of Drosophila chromatin assembly factor 1 is homologous to a histone deacetylase-associated protein.

1996 ◽  
Vol 16 (11) ◽  
pp. 6149-6159 ◽  
Author(s):  
J K Tyler ◽  
M Bulger ◽  
R T Kamakaka ◽  
R Kobayashi ◽  
J T Kadonaga
Keyword(s):  
Drosophila Melanogaster ◽  
Dna Replication ◽  
Histone Modification ◽  
Molecular Mass ◽  
Histone Deacetylase ◽  
Nuclear Extract ◽  
Chromatin Assembly ◽  
Chromatin Assembly Factor ◽  
Assembly Factor

To gain a better understanding of DNA replication-coupled chromatin assembly, we have isolated the cDNA encoding the smallest (apparent molecular mass, 55 kDa; termed p55) subunit of Drosophila melanogaster chromatin assembly factor 1 (dCAF-1), a multisubunit protein that is required for the assembly of nucleosomes onto newly replicated DNA in vitro. The p55 polypeptide comprises seven WD repeat motifs and is homologous to the mammalian RbAp48 protein, which is associated with the HD1 histone deacetylase. dCAF-1 was immunopurified by using affinity-purified antibodies against p55; the resulting dCAF-1 preparation possessed the four putative subunits of dCAF-1 (p180, p105, p75, and p55) and was active for DNA replication-coupled chromatin assembly. Moreover, dCAF-1 activity was specifically depleted with antibodies against p55. Thus, p55 is an integral component of dCAF-1. p55 is localized to the nucleus and is present throughout Drosophila development. Consistent with the homology between p55 and the HD1-associated RbAp48 protein, histone deacetylase activity was observed to coimmunoprecipitate specifically with p55 from a Drosophila nuclear extract. Furthermore, a fraction of the p55 protein becomes associated with the newly assembled chromatin following DNA replication. These findings collectively suggest that p55 may function as a link between DNA replication-coupled chromatin assembly and histone modification.

scholarly journals Hybrid protein assembly-histone modification mechanism for PRC2-based epigenetic switching and memory

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Cecilia Lövkvist ◽  
Pawel Mikulski ◽  
Svenja Reeck ◽  
Matthew Hartley ◽  
Caroline Dean ◽  
...  
Keyword(s):  
Dna Replication ◽  
Histone Modification ◽  
Epigenetic Inheritance ◽  
Memory Storage ◽  
Cell Cycles ◽  
Polycomb Repressive Complex 2 ◽  
Epigenetic State ◽  
State Switching ◽  
Protein Memory ◽  
Switching Memory

The histone modification H3K27me3 plays a central role in Polycomb-mediated epigenetic silencing. H3K27me3 recruits and allosterically activates Polycomb Repressive Complex 2 (PRC2), which adds this modification to nearby histones, providing a read/write mechanism for inheritance through DNA replication. However, for some PRC2 targets, a purely histone-based system for epigenetic inheritance may be insufficient. We address this issue at the Polycomb target FLOWERING LOCUS C (FLC) in Arabidopsis thaliana, as a narrow nucleation region of only ~three nucleosomes within FLC mediates epigenetic state switching and subsequent memory over many cell cycles. To explain the memory’s unexpected persistence, we introduce a mathematical model incorporating extra protein memory storage elements with positive feedback that persist at the locus through DNA replication, in addition to histone modifications. Our hybrid model explains many features of epigenetic switching/memory at FLC and encapsulates generic mechanisms that may be widely applicable.

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