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Figure 6.

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Speculative model for the interaction of Ndc10p, CBF3, and nucleosomes with yeast centromeres. Three different modes of Ndc10p–DNA interaction are shown. The extended CBF3 complex on CDEIII involves sequence-specific binding by one Ndc10p dimer (marked A) and sequence-independent binding by a second dimer (marked B; Espelin et al., 1997 blue right-pointing triangle; Russell et al., 1999 blue right-pointing triangle). We propose that multiple Ndc10p dimers bind sequence-selectively to CDEII (marked C), with particularly important binding by one dimer (C, solid outline) to positions 49–60 of CDEII (Figure 2). The sites of cross-linking by CBF3 subunits to bases in CDEIII are indicated by arrows (Espelin et al., 1997 blue right-pointing triangle). This CBF3–Ndc10p–CEN DNA complex is proposed to be flanked by nuclease hypersensitive sites and embedded in a region of phased nucleosomes that contain the specialized H3 protein Cse4p (Bloom and Carbon, 1982 blue right-pointing triangle; Bloom et al., 1983 blue right-pointing triangle; Funk et al., 1989). No attempt has been made to speculate on the overall folding of centromeric chromatin, but it seems likely from studies in other organisms that it adopts a special structure.

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