| Summary: | Heterochromatin is a repressive chromatin compartment essential for maintaining genomic integrity. A hallmark of heterochromatin is the presence of specialized nonhistone proteins that alter chromatin structure to inhibit transcription and recombination. It is generally assumed that heterochromatin is highly condensed. However, surprisingly little is known about the structure of heterochromatin or its dynamics in solution. In budding yeast, formation of heterochromatin at telomeres and the HM silent mating type loci require the Sir3 protein. Here, we use a combination of sedimentation velocity, atomic force microscopy, and nucleosomal array capture to characterize the stoichiometry and conformation of Sir3 nucleosomal arrays. The results indicate that Sir3 interacts with nucleosomal arrays with a stoichiometry of two Sir3 monomers per nucleosome. We also find that Sir3 fibers are less compact than canonical – magnesium-induced 30 nm fibers. We suggest that heterochromatin proteins promote silencing by “coating” nucleosomal arrays, stabilizing interactions between nucleosomal histones and DNA.
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