Homodimers of chromosomal proteins HMG-14 and HMG-17 in nucleosome cores.

In this work, we report that nucleosome core particles interact with an equimolar mixture of the chromosomal proteins HMG-14 and HMG-17 to form, exclusively, complexes containing two molecules of either HMG-14 or HMG-17 (homodimers). Analysis of the binding of various mixtures of wild-type proteins and their deletion mutants indicates that homodimer formation is not dependent on contacts between the nucleosome-bound HMG-14/-17 proteins themselves. We suggest that HMG-14/-17 proteins in nucleosomes cross-talk by inducing specific allosteric transitions in the chromatin subunit.