Full paperModulation of histone H3 variant synthesis during the myoblast-myotube transition of chicken myogenesis☆
References (25)
- et al.
Isolation and purification of myotube and myoblast nuclei from cultures of embryonic chick skeletal muscle
Exp. Cell Res
(1978) The cyanogen bromide reaction
Re-examination of histone changes during development of newt embryos
Exp. Cell Res
(1978)- et al.
Differentiation of creatine phosphokinase during myogenesis: Quantitative fractionation of isozymes
Dev. Biol
(1977) - et al.
Change in a nuclear phosphoprotein during in vitro myogenesis
Exp. Cell Res
(1978) - et al.
Histone subtypes and switches in synthesis of histone subtypes during Ilyanassa development
Dev. Biol
(1982) - et al.
Isolation and characterization of nuclei and purification of chromatin from differentiating cultures of rat skeletal muscle
Exp. Cell Res
(1982) - et al.
Specific alterations in the pattern of histone-3 synthesis during conversion of human leukemic cells to terminally differentiated cells in culture
Differentiation
(1984) - et al.
Changes in nucleosomal core histone variants during chicken development and maturation
Dev. Biol
(1983) - et al.
Separation of basal histone synthesis from S-phage histone synthesis in dividing cells
Cell
(1981)
Patterns of histone variant synthesis can distinguish G0 from G1 cells
Cell
Synthesis and ubiquitination of histones during myogenesis
Dev. Biol
Cited by (32)
Polyadenylation of Histone H3.1 mRNA Promotes Cell Transformation by Displacing H3.3 from Gene Regulatory Elements
2020, iScienceCitation Excerpt :Polyadenylated canonical histone H3.1 mRNA could induce genomic instability and cell transformation by disrupting the balance between canonical and variant histones. Deposition of canonical histone H3.1 is coupled with DNA replication, and its expression is largely limited to the S phase of the cell cycle, whereas histone variant H3.3 is expressed throughout the cell cycle independent of DNA replication (Brown et al., 1985; Green et al., 2005; Tagami et al., 2004; Wu et al., 1982; Wunsch and Lough, 1987). Polyadenylated canonical H3.1 mRNAs following arsenic exposure were increased during S phase and were also presented outside of S phase (Brocato et al., 2014).
Temporal regulation of chromatin during myoblast differentiation
2017, Seminars in Cell and Developmental BiologyCitation Excerpt :Variants of three of the four core histones (H2A, H2B, H3) exist and play specialized roles in different biological processes. To date, there is no evidence for a role for H2B variants in myogenesis [42]. Replacement of canonical histones with histone variants of H2A and H3 contributes to the regulation of gene expression during skeletal muscle differentiation.
Centromeric chromatin and the pathway that drives its propagation
2012, Biochimica et Biophysica Acta - Gene Regulatory MechanismsCitation Excerpt :New CENP-A protein is synthesized after S phase in G2 and deposited later during mitotic exit and following G1 in human cells and fruit fly embryos [39,80,82–84]. This cell cycle timing is distinct from the H3 variants found in bulk chromatin, H3.1 (canonical H3), H3.2, and H3.3 [85–88]. H3.1/H3.2 are both synthesized and deposited into chromatin during S phase [85,89,90], and associate with CAF-1 [91–94], a chromatin assembly factor that associates with PCNA [95], the sliding DNA clamp used during DNA synthesis [96].
Histone Variants in Metazoan Development
2010, Developmental CellCitation Excerpt :Neurons in the mammalian central nervous system are postmitotic, and several lines of evidence suggest that macroH2A, H3.3, and H2AX are likely to play important roles in neuronal biology. h3.3A RNA and protein levels are observed to increase in multiple models of cell differentiation (Krimer et al., 1993; Lord et al., 1990; Wu et al., 1982; Wunsch and Lough, 1987). High levels of H3.3 protein have been found in differentiating rat neurons, and H3.3 has been shown to be the dominant H3 protein in rat cortical neurons (Bosch and Suau, 1995; Pina and Suau, 1987; Scaturro et al., 1995).
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This work was supported by NIH Grants AM 34679 and HD 20743.
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A.M.W. was supported by a Predoctoral Fellowship from the American Heart Association, Wisconsin Affiliate.