tAlthough the crystal structure of nucleosome core particle is essentially
symmetrical in the vicinity of the dyad, the linker histone binds asymmetri
cally in this region to select a single high-affinity site from potentially
two equivalent sites. To try to resolve this apparent paradox we mapped to
basepair resolution the dyads and rotational settings of nucleosome core p
articles reassembled on synhetic tandemly repeating 20 bp DNA sequences. In
agreement with previous observations, we observed(1) that the helical repe
at on each side of the dyad cluster is 10 bp maintaining register with the
sequence repeat and (2) that this register changes by 2 bp in the vicinity
of the dyad. The additional 2 bp required to effect the change in the rotat
ional settings is accommodated by an adjustment immediately adjacent to the
dyad. At the dyad the hydroxyl radical cleavage is asymmetric and we sugge
st that the inferred structural asymmetry could direct the binding of the l
inker histone to a single preferred site.