A dual role of linker histone H1.4 Lys 34 acetylation in transcriptional activation

Kamieniarz, Kinga; Izzo, Annalisa; Dundr, Miroslav; Tropberger, Philipp; Ozretić, Luka; Kirfel, Jutta; Scheer, Elisabeth; Tropel, Philippe; Wiśniewski, Jacek R.; Tora, Làszlò; Viville, Stéphane; Buettner, Reinhard; Schneider, Robert

doi:10.1101/gad.182014.111

Cited by 84 publications

(73 citation statements)

References 38 publications

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“…Despite the fact that linker histone subtypes act as redundant proteins in knock-out mice (30,33), new data show that each tissue is characterized by a specific set of expressed linker histone subtypes (27,52,53). The globular central domain of the linker histone is highly conserved among the subtypes, but the N-and C-terminal domains are divergent with the C-terminal domain showing especially strong variations in its length and charge.…”

Section: Discussionmentioning

confidence: 99%

Developmentally Regulated Linker Histone H1c Promotes Heterochromatin Condensation and Mediates Structural Integrity of Rod Photoreceptors in Mouse Retina

Popova

Grigoryev

Fan

et al. 2013

Journal of Biological Chemistry

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Background: Heterochromatin condenses in the middle of rod cell nuclei during retina maturation. Results: The level of linker histone H1c increases during retina maturation. Rod photoreceptors in triple H1 knock-out mice have less compact chromatin. Conclusion: H1c is a key architectural factor for chromatin condensation in the rod photoreceptor. Significance: Histone H1c expression may be genetically modified to promote rod photoreceptor maturation and retina integrity.Mature rod photoreceptor cells contain very small nuclei with tightly condensed heterochromatin. We observed that during mouse rod maturation, the nucleosomal repeat length increases from 190 bp at postnatal day 1 to 206 bp in the adult retina. At the same time, the total level of linker histone H1 increased reaching the ratio of 1.3 molecules of total H1 per nucleosome, mostly via a dramatic increase in H1c. Genetic elimination of the histone H1c gene is functionally compensated by other histone variants. However, retinas in H1c/H1e/H1 0 triple knock-outs have photoreceptors with bigger nuclei, decreased heterochromatin area, and notable morphological changes suggesting that the process of chromatin condensation and rod cell structural integrity are partly impaired. In triple knock-outs, nuclear chromatin exposed several epigenetic histone modification marks masked in the wild type chromatin. Dramatic changes in exposure of a repressive chromatin mark, H3K9me2, indicate that during development linker histone plays a role in establishing the facultative heterochromatin territory and architecture in the nucleus. During retina development, the H1c gene and its promoter acquired epigenetic patterns typical of rod-specific genes. Our data suggest that histone H1c gene expression is developmentally up-regulated to promote facultative heterochromatin in mature rod photoreceptors.During mammalian development, cells committed to differentiate into a specific tissue withdraw from the cell cycle and start a process of tissue maturation that involves up-regulation of genes specific for the differentiated tissue and down-regulation of genes specific for progenitor cells (1, 2). This developmentally regulated process culminates in formation of compact blocks of heterochromatin inside the nuclei and spatial segregation of heterochromatin and euchromatin domains (3). Chromatin condensation prevents certain transcription factors from activating genes in the compact chromatin (4). Recent studies suggest that each tissue type has its own unique program that orchestrates tissue maturation, with specific sets of chromatin architectural and remodeling proteins, histone modifications, and micro-RNA (5-12).The mammalian retina is a part of the CNS and is derived from the optic cup, an outgrowth of forebrain neuroepithelium formed early in CNS development. Six major neuronal and one glial cell types are generated from the multipotential retinal progenitors in a stereotypic temporal sequence. In mice the terminal differentiation of retinal cells spans from embryonic day ...

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Section: Discussionmentioning

confidence: 99%

Developmentally Regulated Linker Histone H1c Promotes Heterochromatin Condensation and Mediates Structural Integrity of Rod Photoreceptors in Mouse Retina

Popova

Grigoryev

Fan

et al. 2013

Journal of Biological Chemistry

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“…Is this a relevant in vivo activity? Future studies will address this, but it is worth mentioning that a recent study showed that human Gcn5 acetylates H1.4 at K34ac during transcription activation (63). Keeping in mind its evolutionary relationship with Rtt109, it will be interesting to determine whether p300/CBP also acetylates linker histone.…”

Section: Discussionmentioning

confidence: 99%

The Carboxyl Terminus of Rtt109 Functions in Chaperone Control of Histone Acetylation

et al. 2013

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e Rtt109 is a fungal histone acetyltransferase (HAT) that catalyzes histone H3 acetylation functionally associated with chromatin assembly. Rtt109-mediated H3 acetylation involves two histone chaperones, Asf1 and Vps75. In vivo, Rtt109 requires both chaperones for histone H3 lysine 9 acetylation (H3K9ac) but only Asf1 for full H3K56ac. In vitro, Rtt109-Vps75 catalyzes both H3K9ac and H3K56ac, whereas Rtt109-Asf1 catalyzes only H3K56ac. In this study, we extend the in vitro chaperone-associated substrate specificity of Rtt109 by showing that it acetylates vertebrate linker histone in the presence of Vps75 but not Asf1. In addition, we demonstrate that in Saccharomyces cerevisiae a short basic sequence at the carboxyl terminus of Rtt109 (Rtt109C) is required for H3K9ac in vivo. Furthermore, through in vitro and in vivo studies, we demonstrate that Rtt109C is required for optimal H3K56ac by the HAT in the presence of full-length Asf1. When Rtt109C is absent, Vps75 becomes important for H3K56ac by Rtt109 in vivo. In addition, we show that lysine 290 (K290) in Rtt109 is required in vivo for Vps75 to enhance the activity of the HAT. This is the first in vivo evidence for a role for Vps75 in H3K56ac. Taken together, our results contribute to a better understanding of chaperone control of Rtt109-mediated H3 acetylation.

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“…recently beginning to be appreciated. Of particular note is acetylation of a conserved lysine at position 34 on histone H1.4 (H1.4K34Ac), which is associated with increased H1 mobility and transcriptional activation (26). Compared with the core histones, which remain in place for several hours, H1 proteins are substantially more mobile with a mean residence time at any one binding site estimated to be ϳ3 min (43), albeit less mobile than transcription factors that boast mean residence times of 5-25 s (44).…”

Section: Discussionmentioning

confidence: 99%

“…It is noteworthy that Lys-34 in histone H1.2/1.3-the peptide KASGPPVSELITK being common to both histone variants-is also subject to acetylation, monomethylation, and formylation (25). Interestingly, the same lysine residue is also acetylated in histone variant H1.4 (H1.4K34Ac), a modification recently shown to be associated with transcriptional activation (26).…”

Section: Cps1 Is Required For Nuclear Proteinmentioning

confidence: 99%

Homocitrullination Is a Novel Histone H1 Epigenetic Mark Dependent on Aryl Hydrocarbon Receptor Recruitment of Carbamoyl Phosphate Synthase 1

Joshi

Mustafa²,

Lichti

et al. 2015

Journal of Biological Chemistry

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Background: Characterization of a Nonconsensus xenobiotic response element (NC-XRE), a novel AhR binding site. Results: AhR binding to the NC-XRE in response to TCDD results in the recruitment of CPS1 and concomitant homocitrullination of histone H1. Conclusion: CPS1-mediated homocitrullination of histone H1 on lysine 34 is a novel epigenetic mark. Significance: Homocitrulline (hcit) is a novel epigenetic histone mark involved in chromatin remodeling and transcriptional activation.

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A dual role of linker histone H1.4 Lys 34 acetylation in transcriptional activation

Cited by 84 publications

References 38 publications

Developmentally Regulated Linker Histone H1c Promotes Heterochromatin Condensation and Mediates Structural Integrity of Rod Photoreceptors in Mouse Retina

Developmentally Regulated Linker Histone H1c Promotes Heterochromatin Condensation and Mediates Structural Integrity of Rod Photoreceptors in Mouse Retina

The Carboxyl Terminus of Rtt109 Functions in Chaperone Control of Histone Acetylation

Homocitrullination Is a Novel Histone H1 Epigenetic Mark Dependent on Aryl Hydrocarbon Receptor Recruitment of Carbamoyl Phosphate Synthase 1

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