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Fig. 7. NAP-1 functions as a chaperone for linker histone B4. Reconstituted dinucleosomes (4 nM) were incubated with B4 or B4/NAP-1 complex and analyzed by agarose gel electrophoresis. Free DNA, dinucleosomes, and one and two molecules of B4 per dinucleosome are indicated. More histone B4 was bound to the dinucleosome when B4 alone was added than when an equivalent concentration of B4/NAP-1 was added. In the absence of NAP-1, the resulting dinucleosome-B4 complexes gave smeared bands and were partially retained at the gel top.

Fig. 8. Binding of histones B4 and H1A to dinucleosomes without NAP-1 leads to inhibition of ACF-dependent chromatin remodeling. Each sample was analyzed for chromatin remodeling as shown in Fig. 2, except for assembly of B4 (A) and H1A (B) without NAP-1. End-radiolabeled dinucleosomes (4 nM) were incubated with linker histones. The binding of B4 or H1A to dinucleosomes gave rise to smeared bands on agarose gels (lanes 1-4). The extent of digestion of the 5' RsaI restriction site is shown at the bottom of each lane (lanes 5-12). Chromatin remodeling was completely inhibited upon the binding of linker histones to dinucleosomes.