Solution-state conformation and stoichiometry of yeast Sir3 heterochromatin fibres

Sarah G. Swygert, Benjamin J. Manning, Subhadip Senapati, Parminder Kaur, Stuart Lindsay, Borries Demeler and Craig L. Peterson ()
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Sarah G. Swygert: Program in Molecular Medicine, University of Massachusetts Medical School
Benjamin J. Manning: Program in Molecular Medicine, University of Massachusetts Medical School
Subhadip Senapati: Center for Single Molecule Biophysics, Biodesign Institute, Arizona State University
Parminder Kaur: Center for Single Molecule Biophysics, Biodesign Institute, Arizona State University
Stuart Lindsay: Center for Single Molecule Biophysics, Biodesign Institute, Arizona State University
Borries Demeler: University of Texas Health Sciences Center
Craig L. Peterson: Program in Molecular Medicine, University of Massachusetts Medical School

Nature Communications, 2014, vol. 5, issue 1, 1-12

Abstract: Abstract 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 homothallic 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 fibres are less compact than canonical magnesium-induced 30 nm fibres. We suggest that heterochromatin proteins promote silencing by ‘coating’ nucleosomal arrays, stabilizing interactions between nucleosomal histones and DNA.

Date: 2014
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DOI: 10.1038/ncomms5751

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