PARP1 found to directly disassemble nucleosomes during DNA repair
Start here
PARP1, an enzyme already central to DNA damage response and a target of cancer therapy, has been shown to directly disassemble nucleosomes, the packaging units of chromatin. In work published in Molecular Cell, PARP1 promotes NAD+-dependent removal of H2A-H2B dimers from nucleosomes, generating oriented hexasomes with higher DNA accessibility. The H2A C-terminal tail supports this remodeling activity. The findings establish a direct mechanical link between PARP1 and chromatin opening, connecting PARP1-dependent nucleosome disassembly to the cellular response to DNA damage. Open questions include how this remodeling activity is coordinated with other DNA repair factors in cells and what it implies for the action of PARP inhibitors.
Written by a model from the reports · updated 4 hours ago
Coverage timeline
Follow the coverage to see the different angles.
- cell.comPickPARP1 directly disassembles nucleosomes to regulate DNA repair
PARP1 directly disassembles nucleosomes by promoting NAD+-dependent removal of H2A-H2B dimers, generating oriented hexasomes with increased DNA accessibility. The H2A C-terminal tail supports this remodeling activity, linking PARP1-dependent nucleosome disassembly to cellular responses to DNA damage.
Heat trend for this story
Heat now 6·Peak in the comparable set 10 (Oct 23 08:00)·Change over 24h in the comparable set –·Participants now 1
Participants counted above, heat below. The trend compares only the participants observed in full throughout, so its set can be smaller than the heat figure itself. Move the pointer or click the chart for an hour's reading; the left and right arrow keys work too.