- Abstract:
-
Poly(ADP-ribosyl)ation plays a major role in DNA repair, where it regulates chromatin relaxation as one of the critical events in the repair process. However, the molecular mechanism by which poly(ADP-ribose) modulates chromatin remains poorly understood. Here we identify the poly(ADP-ribose)-regulated protein APLF as a DNA-damage-specific histone chaperone. APLF preferentially binds to the histone H3/H4 tetramer via its C-terminal acidic motif, which is homologous to the motif conserved in t...
Expand abstract - Publisher copy:
- 10.1016/j.molcel.2010.12.008
-
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- Journal:
- Molecular cell
- Volume:
- 41
- Issue:
- 1
- Pages:
- 46-55
- Publication date:
- 2011-01-05
- DOI:
- EISSN:
-
1097-4164
- ISSN:
-
1097-2765
- URN:
-
uuid:e24931ee-a3a2-4bed-8e56-12b1ab8c881d
- Source identifiers:
-
376187
- Local pid:
- pubs:376187
- Language:
- English
- Keywords:
- Copyright date:
- 2011
Journal article
DNA repair factor APLF is a histone chaperone.
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