Fink M, et al. (2007) Contribution of the Serine 129 of Histone H2A to Chromatin Structure. Mol Cell Biol 27(10):3589-600
Abstract: Phosphorylation of a yeast histone H2A at the C-terminal serine 129 has a central role in double-strand break repair. Mimicking H2A phosphorylation by replacement of serine 129 with glutamic acid (hta1-S129E) suggested that phosphorylation destabilizes chromatin structures and thereby facilitates access of repair proteins. Here, we have tested chromatin structures in hta1-S129 mutants and in a C-terminal tail deletion strain. We show that the hta1-S129E affects neither nucleosome positioning in minichromosomes and genomic loci nor supercoiling of minichromosomes. Moreover, hta1-S129E has no effect on chromatin stability measured by conventional nuclease digestion nor does it affect DNA accessibility and repair of UV-induced DNA lesions by nucleotide excision repair and photolyase in vivo. Similarly, deletion of the C-terminal tail has no effect on nucleosome positioning and stability. These data argue against a general role of the C-terminal tail in chromatin organization and suggest that phosphorylated H2A, gamma-H2AX in higher eukaryotes, acts by recruitment of repair components rather than by destabilizing chromatin structures.
|Status: Published||Type: Journal Article||PubMed ID: 17353265|
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