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Human Asf1 and CAF-1 interact and synergize in a repair-coupled nucleosome assembly pathway

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Nigg,  E. A.
Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Mello, J. A., Sillje, H. H. W., Roche, D. M. J., Kirschner, D. B., Nigg, E. A., & Almouzni, G. (2002). Human Asf1 and CAF-1 interact and synergize in a repair-coupled nucleosome assembly pathway. EMBO Reports, 3(4), 329-334.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6F78-9
Abstract
The efficient assembly of newly replicated and repaired DNA into chromatin is essential for proper genome function. Based on genetic studies in Saccharomyces cerevisiae, the histone chaperone anti-silencing function 1 (Asf1) has been implicated in the DNA repair response. Here, the human homologs are shown to function synergistically with human CAF-1 to assemble nucleosomes during nucleotide excision repair in vitro. Furthermore, we demonstrate that hAsf1 proteins can interact directly with the p60 subunit of hCAF-1. In contrast to hCAF-1 p60, the nuclear hAsf1 proteins are not significantly associated with chromatin in cells before or after the induction of DNA damage, nor specifically recruited to damaged DNA during repair in a bead-linked DNA assay. A model is proposed in which the synergism between hAsf1 and CAF-1 for nucleosome formation during DNA repair is achieved through a transient physical interaction allowing histone delivery from Asf1 to CAF-1.