Abstract
We have purified uH2A (A24) and reconstituted it, in place of H2A, into high molecular weight nucleohistone containing the core histones and DNA. uH2A-containing core particles were then prepared by nuclease digestion and studies on these particles were carried out. We show that two uH2A molecules can be accommodated within a core particle. We also show that the presence of two uH2A molecules in a core particle does not alter significantly either the pattern or the rate of DNase I digestion as compared to both reconstituted and native core particles. Finally, we show that HMG proteins 14 and 17 can bind to uH2A-containing core particles. We conclude that uH2A has little influence on structure at the level of individual nucleosomes.
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