Heparin binds to intact mononucleosomes and induces a novel unfolded structure.

It has been previously shown that heparin can bind to chromatin and enhance transcriptional activity. To characterize this phenomenon further, we have studied the interaction of heparin with isolated core mononucleosomes from avian reticulocytes. The results of these studies suggest that heparin bound reversibly to intact core mononucleosomes to induce a new structure, identified by decreased electrophoretic mobility and altered circular dichroism spectra. This altered nucleosome conformation exhibits 3-5-fold increased sensitivity to digestion by the nuclease, DNase I, and allows more efficient passage of RNA polymerase. At higher concentrations of heparin, core histones were completely removed from DNA. The finding of a reversible nucleosome-heparin complex in which core DNA is readily accessible to both RNA polymerase and the nuclease DNase I is discussed in the context of transcriptionally active chromatin.