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American Association for the Advancement of Science, Science, 6258(350), 2015

DOI: 10.1126/science.aac4383

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Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2

Journal article published in 2015 by Lianying Jiao, Xin Liu ORCID
This paper is available in a repository.
This paper is available in a repository.

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Abstract

A tripartite gene silencing complex The formation of specialized cell types during development involves the silencing of genes not required in those cell types. An important player in this silencing process is the polycomb repressive complex 2 (PRC2), which methylates histone H3 on lysine residue 27 (H3K27me). Jiao and Liu determined the x-ray crystal structure of a functional PRC2 complex from a thermophilic yeast species (see the Perspective by Schapira). The intimate association of the three subunits confers stability to PRC2. The structure also reveals how the reaction product, H3K27me, stimulates PRC2 allosterically and how a cancer-associated histone mutation blocks the PRC2 active site. Science , this issue p. 10.1126/science.aac4383 ; see also p. 278