Chromatin assembly and signalling the end of DNA repair requires acetylation of histone H3 on lysine 56.
The packaging of DNA into chromatin results in a barrier to all DNA transactions. To facilitate transcription, replication and repair histone proteins are frequently post-translational modified. Such covalent additions to histone residues can modulate chromatin folding and/or provide specificity to docking surfaces for non-histone chromatin proteins. In the budding yeast, one such modification, transient acetylation of histone H3 on residue lysine 56 (H3K56ac); occurs on newly synthesized H3 molecules and facilitates their deposition onto newly replicated DNA during S phase. H3K56ac also has a role in chromatin reassembly following DNA damage in S phase. Importantly, the completion of H3K56ac-dependent chromatin reassembly appears to be required for resumption of cell proliferation after DNA repair. Emerging evidence, although not without conflict, suggests that H3K56ac is not only present in human cells, but is similarly regulated and required for chromatin reassembly.
Costelloe
Thomas
T
Centre for Chromosome Biology, School of Natural Sciences, National University of Ireland, Galway, Galway, Ireland.
Lowndes
Noel F
NF
D000107:Acetylation; D002843:Chromatin / Q000378:metabolism*; D004260:DNA Repair; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008239:Lysine / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D015398:Signal Transduction
D002843:Chromatin; D006657:Histones; D008239:Lysine