Modulation of histone H3 variant synthesis during the myoblast-myotube transition of chicken myogenesis

Wunsch, Ann M.; Lough, John

doi:10.1016/0012-1606(87)90210-7

Cited by 34 publications

(30 citation statements)

References 22 publications

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“…1B) (1,27). Consistent with the expression pattern of HIRA, two mouse H3.3 genes, H3.3a and H3.3b, were continuously expressed as previously reported in chicken myogenesis (28), whereas canonical H3s (H3.1s and H3.2s) and other variant histones, macroH2A, H2A.X, H2A.Z, and CENP-A, were down-regulated after withdrawal from the cell cycle ( Fig. 1 A and C and Fig.…”

Section: Differential Expression Of Rc and Ri Components During Myoblastsupporting

confidence: 86%

Myogenic transcriptional activation of MyoD mediated by replication-independent histone deposition

Yang

Song

Seol

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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In mammals, the canonical histone H3 and the variant H3.3 are assembled into chromatin through replication-coupled and replication-independent (RI) histone deposition pathways, respectively, to play distinct roles in chromatin function. H3.3 is largely associated with transcriptionally active regions via the activity of RI histone chaperone, HIRA. However, the precise role of the RI pathway and HIRA in active transcription and the mechanisms by which H3.3 affects gene activity are not known. In this study, we show that HIRA is an essential factor for muscle development by establishing MyoD activation in myotubes. HIRA and Asf1a, but not CHD1 or Asf1b, mediate H3.3 incorporation in the promoter and the critical upstream regulatory regions of the MyoD gene. HIRA and H3.3 are required for epigenetic transition into the more permissive chromatin structure for polymerase II recruitment to the promoter, regardless of transcription-associated covalent modification of histones. Our results suggest distinct epigenetic management of the master regulator with RI pathway components for cellular differentiation.

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Section: Differential Expression Of Rc and Ri Components During Myoblastsupporting

confidence: 86%

Myogenic transcriptional activation of MyoD mediated by replication-independent histone deposition

Yang

Song

Seol

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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“…Also, histone H3.3 accumulates in nondividing, differentiated cells and fibroblasts approaching senescence, in some cases to ca. 90% of the total histone H3, with presumably the majority being in inactive chromatin (5,6,13,22,44,47,52,65,71). Moreover, upon egg fertilization in flies and worms, the sperm chromatin is remodeled prior to DNA replication using histone variant H3.3, seemingly in a transcription-independent manner (28,42).…”

Section: Discussionmentioning

confidence: 99%

HP1 Proteins Are Essential for a Dynamic Nuclear Response That Rescues the Function of Perturbed Heterochromatin in Primary Human Cells

Zhang

Liu

Chen

et al. 2007

Molecular and Cellular Biology

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Cellular information is encoded genetically in the DNA nucleotide sequence and epigenetically by the "histone code," DNA methylation, and higher-order packaging of DNA into chromatin. Cells possess intricate mechanisms to sense and repair damage to DNA and the genetic code. However, nothing is known of the mechanisms, if any, that repair and/or compensate for damage to epigenetically encoded information, predicted to result from perturbation of DNA and histone modifications or other changes in chromatin structure. Here we show that primary human cells respond to a variety of small molecules that perturb DNA and histone modifications by recruiting HP1 proteins to sites of altered pericentromeric heterochromatin. This response is essential to maintain the HP1-binding kinetochore protein hMis12 at kinetochores and to suppress catastrophic mitotic defects. Recruitment of HP1 proteins to pericentromeres depends on histone H3.3 variant deposition, mediated by the HIRA histone chaperone. These data indicate that defects in pericentromeric epigenetic heterochromatin modifications initiate a dynamic HP1-dependent response that rescues pericentromeric heterochromatin function and is essential for viable progression through mitosis.The eukaryotic genome is packaged into the cell nucleus in the form of chromatin, a composite of DNA, RNA, and protein. The basic repeating unit of chromatin structure is the core nucleosome, comprised of eight histone protein molecules and 146 bp of DNA. Nucleosomes are folded into multiple higher levels of organization, together with other proteins and RNA, to form chromatin (16). In chromatin, a complex array of histone modifications, histone variants, associated proteins, RNAs, higher-order folding conformations, and site-specific DNA methylation controls DNA accessibility and recruitment of specific regulatory molecules, thereby regulating most DNA functions, including transcription, replication, recombination, and repair. For example, histone acetylation acts to open up chromatin, thereby promoting transcription, and also recruits specific transcription activators, such as Brg1, through interactions between acetylated histones and bromodomains in the protein module (29).Information that is not directly coded by the DNA sequence but instead is encoded by DNA methylation, histone modifications, or other aspects of chromatin structure, is epigenetically determined. The histone modifications that contribute to epigenetic information have been proposed to constitute a histone code, by analogy to the genetic code (68). Cells possess elaborate mechanisms to sense and repair damage to the genetic code (19). Extending the analogy between the genetic code and the histone code, if histone and DNA modifications encode information outside of the DNA sequence, the cell is likely to have mechanisms to sense and repair, or otherwise respond to, alterations in these modifications. How cells respond to alteration of chromatin and epigenetic modifications is poorly understood.Kinetochores are large macromole...

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“…HIRA-containing chaperone complexes preferentially deposit the histone variant histone H3.3, over the canonical histone H3.1, in a DNA replication-independent manner (72,125). Significantly, histone H3.3 accumulates in fibroblasts approaching senescence and in non-dividing differentiated cells, in some cases to about 90% of the total histone H3, with presumably the majority being in inactive chromatin (15,18,52,68,92,98,106,128,137). Unfortunately, because human histone H3.3 and canonical H3.1 only differ by 5 amino-acids, differentiating between them immunologically is challenging, making it difficult to ask whether endogenous histone H3.3 is specifically enriched in SAHF.…”

Section: Chromosome Condensation Is Driven By Histone Chaperones Hiramentioning

confidence: 99%

Remodeling of chromatin structure in senescent cells and its potential impact on tumor suppression and aging

Adams

2007

Gene

161

135

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Cellular senescence is an important tumor suppression process, and a possible contributor to tissue aging. Senescence is accompanied extensive changes in chromatin structure. In particular, many senescent cells accumulate specialized domains of facultative heterochromatin, called Senescence Associated Heterochromatin Foci (SAHF), which are thought to repress expression of proliferationpromoting genes, thereby contributing to senescence-associated proliferation arrest. This article reviews our current understanding of the structure, assembly and function of these SAHF at a cellular level. The possible contribution of SAHF to tumor suppression and tissue aging is also critically discussed.

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Modulation of histone H3 variant synthesis during the myoblast-myotube transition of chicken myogenesis

Cited by 34 publications

References 22 publications

Myogenic transcriptional activation of MyoD mediated by replication-independent histone deposition

Myogenic transcriptional activation of MyoD mediated by replication-independent histone deposition

HP1 Proteins Are Essential for a Dynamic Nuclear Response That Rescues the Function of Perturbed Heterochromatin in Primary Human Cells

Remodeling of chromatin structure in senescent cells and its potential impact on tumor suppression and aging

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