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.
|Evidence ID||Analyze ID||Interactor||Interactor Systematic Name||Interactor||Interactor Systematic Name||Type||Assay||Annotation||Action||Modification||Phenotype||Source||Reference||Note|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Gene Ontology Term||Gene Ontology Term ID||Qualifier||Aspect||Method||Evidence||Source||Assigned On||Reference||Annotation Extension|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Phenotype||Experiment Type||Experiment Type Category||Mutant Information||Strain Background||Chemical||Details||Reference|
|Evidence ID||Analyze ID||Regulator||Regulator Systematic Name||Target||Target Systematic Name||Experiment||Conditions||Strain||Source||Reference|