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Methylation and acetylation of position-specific lysine residues in the N-terminal tail of histones H3 and H4 play an important role in regulating chromatin structure and function. In the case of H3-Lys⁴, H3-Lys⁹, H3-Lys²⁷, and H4-Lys²⁰, the degree of methyla-tion was variable from the mono- to the di- or trimethylated state, each of which was presumed to be involved in the organization of chromatin and the activation or repression of genes. Here we inves-tigated the interplay between histone H4-Lys²⁰ mono- and trim-ethylation and H4 acetylation at induced (β-major/β-minor glo-bin), repressed (c-myc), and silent (embryonic β-globin) genes during in vitro differentiation of mouse erythroleukemia cells. By using chromatin immunoprecipitation, we found that the β-majorand β-minor promoter and the β-globin coding regions as well as the promoter and the transcribed exon 2 regions of the highly expressed c-myc …