Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2
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- Lianying Jiao
- Cecil H. and Ida Green Center for Reproductive Biology Sciences and Division of Basic Research, Department of Obstetrics and Gynecology and Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
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- Xin Liu
- Cecil H. and Ida Green Center for Reproductive Biology Sciences and Division of Basic Research, Department of Obstetrics and Gynecology and Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
書誌事項
- 公開日
- 2015-10-16
- 権利情報
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- http://www.sciencemag.org/about/science-licenses-journal-article-reuse
- DOI
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- 10.1126/science.aac4383
- 公開者
- American Association for the Advancement of Science (AAAS)
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説明
<jats:title>A tripartite gene silencing complex</jats:title> <jats:p>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.</jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" related-article-type="in-this-issue" xlink:href="10.1126/science.aac4383">10.1126/science.aac4383</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6258" page="278" related-article-type="in-this-issue" vol="350" xlink:href="10.1126/science.aad5203">278</jats:related-article> </jats:p>
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- Science
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Science 350 (6258), aac4383-, 2015-10-16
American Association for the Advancement of Science (AAAS)
