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Biochemistry. 1998 Jun 16;37(24):8622-8.

Linker DNA and H1-dependent reorganization of histone-DNA interactions within the nucleosome.

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Department of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, New York 14642, USA.


We have employed a site-directed photochemical cross-linking procedure to precisely map interactions between nucleosomal DNA and the C-terminal tail of core histone H2A. We find that this tail has the potential to contact multiple sites within the nucleosome and that these contacts are dependent upon the configuration of the complex. This tail contacts DNA near the dyad axis within nucleosome core particles but rearranges to a site near the edge of the nucleosomal DNA when linker DNA is present. Moreover, in the presence of linker histone H1 the contacts near the edge of the nucleosome but not at the dyad are further rearranged. In addition, we present further evidence for the suggestion that the binding of linker histone causes a subtle but global change in core histone-DNA interactions within the nucleosome [Usachenko, S. I., Gavin, I. M., and Bavykin, S. G. (1996) J. Biol. Chem. 271, 3831-3836].

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