Chromatin topology is coupled to Polycomb group protein subnuclear organization

Ajazul H. Wani, Alistair N. Boettiger, Patrick Schorderet, Ayla Ergun, Christine Münger, Ruslan I. Sadreyev, Xiaowei Zhuang, Robert E. Kingston and Nicole J. Francis ()
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Ajazul H. Wani: Massachusetts General Hospital
Alistair N. Boettiger: Howard Hughes Medical Institute, Harvard University Cambridge
Patrick Schorderet: Massachusetts General Hospital
Ayla Ergun: Massachusetts General Hospital
Christine Münger: Institut de recherches cliniques de Montréal
Ruslan I. Sadreyev: Massachusetts General Hospital
Xiaowei Zhuang: Howard Hughes Medical Institute, Harvard University Cambridge
Robert E. Kingston: Massachusetts General Hospital
Nicole J. Francis: Institut de recherches cliniques de Montréal

Nature Communications, 2016, vol. 7, issue 1, 1-13

Abstract: Abstract The genomes of metazoa are organized at multiple scales. Many proteins that regulate genome architecture, including Polycomb group (PcG) proteins, form subnuclear structures. Deciphering mechanistic links between protein organization and chromatin architecture requires precise description and mechanistic perturbations of both. Using super-resolution microscopy, here we show that PcG proteins are organized into hundreds of nanoscale protein clusters. We manipulated PcG clusters by disrupting the polymerization activity of the sterile alpha motif (SAM) of the PcG protein Polyhomeotic (Ph) or by increasing Ph levels. Ph with mutant SAM disrupts clustering of endogenous PcG complexes and chromatin interactions while elevating Ph level increases cluster number and chromatin interactions. These effects can be captured by molecular simulations based on a previously described chromatin polymer model. Both perturbations also alter gene expression. Organization of PcG proteins into small, abundant clusters on chromatin through Ph SAM polymerization activity may shape genome architecture through chromatin interactions.

Date: 2016
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DOI: 10.1038/ncomms10291

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