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. Author manuscript; available in PMC: 2012 Sep 17.
Published in final edited form as: Mol Cell. 2011 Jan 7;41(1):46–55. doi: 10.1016/j.molcel.2010.12.008

Figure 1. APLF interacts with core histones.

Figure 1

Complexes were purified by immunoprecipitation of transiently expressed FLAG-tagged proteins in HEK293T cells. A, Schematic representation of the APLF domain structure and detailed alignment of the conserved motif within the acidic C-terminal domain homologous to the NAP1-like family of histone chaperones (NAP1L motif). Various mutant constructs used in the studies are shown separately. Point mutants in the NAP1L motif are indicated by red arrows. B, SyproRuby staining of the immunoprecipitated APLF complex. Relevant interactors identified by mass spectrometry are indicated. C, Immunoblot confirming the interaction of APLF with core histones at low and high salt stringency. D, The interaction of APLF with core histones is independent of poly(ADP-ribosyl)ation. E, Interaction of APLF with core histones is mediated by the acidic C-terminal domain. F, The presence of histones in ALC1-associated complexes is dependent on APLF.