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长距离异染色质的关联是由沉默和双链 DNA 断裂修复蛋白介导的。

Long-range heterochromatin association is mediated by silencing and double-strand DNA break repair proteins.

机构信息

Department of Molecular, Cell and Developmental Biology, University of California, Santa Cruz, Santa Cruz, CA 95064, USA.

出版信息

J Cell Biol. 2013 Jun 10;201(6):809-26. doi: 10.1083/jcb.201211105. Epub 2013 Jun 3.

DOI:10.1083/jcb.201211105
PMID:23733345
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3678155/
Abstract

The eukaryotic genome is highly organized in the nucleus, and this organization affects various nuclear processes. However, the molecular details of higher-order organization of chromatin remain obscure. In the present study, we show that the Saccharomyces cerevisiae silenced loci HML and HMR cluster in three-dimensional space throughout the cell cycle and independently of the telomeres. Long-range HML-HMR interactions require the homologous recombination (HR) repair pathway and phosphorylated H2A (γ-H2A). γ-H2A is constitutively present at silenced loci in unperturbed cells, its localization requires heterochromatin, and it is restricted to the silenced domain by the transfer DNA boundary element. SMC proteins and Scc2 localize to the silenced domain, and Scc2 binding requires the presence of γ-H2A. These findings illustrate a novel pathway for heterochromatin organization and suggest a role for HR repair proteins in genomic organization.

摘要

真核生物基因组在细胞核中高度组织化，这种组织化影响各种核过程。然而，染色质高级组织的分子细节仍然不清楚。在本研究中，我们表明，酿酒酵母沉默的 HML 和 HMR 基因座在整个细胞周期中以及独立于端粒在三维空间中聚集。长距离 HML-HMR 相互作用需要同源重组 (HR) 修复途径和磷酸化的 H2A（γ-H2A）。γ-H2A 在未受干扰的细胞中在沉默的基因座上持续存在，其定位需要异染色质，并且由转移 DNA 边界元件限制在沉默的域中。SMC 蛋白和 Scc2 定位于沉默的域，并且 Scc2 结合需要γ-H2A 的存在。这些发现说明了异染色质组织的新途径，并表明 HR 修复蛋白在基因组组织中的作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f3f/3678155/50a3b7fec0de/JCB_201211105_Fig8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f3f/3678155/2e67f5a13e93/JCB_201211105_Fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f3f/3678155/5e5237c32eb7/JCB_201211105_Fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f3f/3678155/01f9abdb8eee/JCB_201211105_Fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f3f/3678155/46e84a607ab5/JCB_201211105_Fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f3f/3678155/21060234dc04/JCB_201211105_Fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f3f/3678155/4ca957106130/JCB_201211105_Fig6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f3f/3678155/f168ce009c36/JCB_201211105_Fig7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f3f/3678155/50a3b7fec0de/JCB_201211105_Fig8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f3f/3678155/2e67f5a13e93/JCB_201211105_Fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f3f/3678155/5e5237c32eb7/JCB_201211105_Fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f3f/3678155/01f9abdb8eee/JCB_201211105_Fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f3f/3678155/46e84a607ab5/JCB_201211105_Fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f3f/3678155/21060234dc04/JCB_201211105_Fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f3f/3678155/4ca957106130/JCB_201211105_Fig6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f3f/3678155/f168ce009c36/JCB_201211105_Fig7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f3f/3678155/50a3b7fec0de/JCB_201211105_Fig8.jpg

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