期刊
MOLECULAR CELL
卷 41, 期 1, 页码 46-55出版社
CELL PRESS
DOI: 10.1016/j.molcel.2010.12.008
关键词
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资金
- Cancer Research UK
- Wellcome Trust [064414]
- Australian National Health and Medical Research Council
- Biotechnology and Biological Sciences Research Council [BB/E022286/1] Funding Source: researchfish
- BBSRC [BB/E022286/1] Funding Source: UKRI
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 the histone chaperones of the NAP1L family (NAP1L motif). We further demonstrate that APLF exhibits histone chaperone activities in a manner that is dependent on its acidic domain and that the NAP1L motif is critical for the repair capacity of APLF in vivo. Finally, we identify structural analogs of APLF in lower eukaryotes with the ability to bind histones and localize to the sites of DNA-damage-induced poly(ADP-ribosyl)ation. Collectively, these findings define the involvement of histone chaperones in poly(ADP-ribose)-regulated DNA repair reactions.
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