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招募依赖于 ATP 的染色质重塑酶 dMi-2 到活跃的热休克基因转录区。

Recruitment of the ATP-dependent chromatin remodeler dMi-2 to the transcribed region of active heat shock genes.

机构信息

Institute for Molecular Biology and Tumor Research, Philipps-University, Emil-Mannkopff-Strasse 2, 35037 Marburg, Germany.

出版信息

Nucleic Acids Res. 2012 Jun;40(11):4879-91. doi: 10.1093/nar/gks178. Epub 2012 Feb 22.

DOI:10.1093/nar/gks178
PMID:22362736
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3367206/
Abstract

The ATP-dependent chromatin remodeler dMi-2 can play both positive and negative roles in gene transcription. Recently, we have shown that dMi-2 is recruited to the hsp70 gene in a heat shock-dependent manner, and is required to achieve high transcript levels. Here, we use chromatin immunoprecipitation sequencing (ChIP-Seq) to identify other chromatin regions displaying increased dMi-2 binding upon heat shock and to characterize the distribution of dMi-2 over heat shock genes. We show that dMi-2 is recruited to the body of at least seven heat shock genes. Interestingly, dMi-2 binding extends several hundred base pairs beyond the polyadenylation site into the region where transcriptional termination occurs. We find that dMi-2 does not associate with the entire nucleosome-depleted hsp70 locus 87A. Rather, dMi-2 binding is restricted to transcribed regions. Our results suggest that dMi-2 distribution over active heat shock genes are determined by transcriptional activity.

摘要

ATP 依赖的染色质重塑酶 dMi-2 在基因转录中可以发挥正反两方面的作用。最近,我们已经表明,dMi-2 以热休克依赖的方式被招募到 hsp70 基因,并且是实现高转录水平所必需的。在这里,我们使用染色质免疫沉淀测序(ChIP-Seq)来鉴定其他在热休克时显示出 dMi-2 结合增加的染色质区域,并对 dMi-2 在热休克基因上的分布进行特征描述。我们表明,dMi-2 被招募到至少七个热休克基因的主体上。有趣的是,dMi-2 的结合延伸到多聚腺苷酸化位点之外几百个碱基对,进入转录终止发生的区域。我们发现 dMi-2 不与整个无核小体耗尽的 hsp70 基因座 87A 相关联。相反,dMi-2 结合仅限于转录区域。我们的结果表明,dMi-2 在活跃的热休克基因上的分布是由转录活性决定的。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b242/3367206/865a75002e6a/gks178f5a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b242/3367206/58adcdaa4371/gks178f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b242/3367206/48fc6de5f1d5/gks178f2a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b242/3367206/30d108de7e72/gks178f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b242/3367206/3b1303a1ab68/gks178f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b242/3367206/865a75002e6a/gks178f5a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b242/3367206/58adcdaa4371/gks178f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b242/3367206/48fc6de5f1d5/gks178f2a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b242/3367206/30d108de7e72/gks178f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b242/3367206/3b1303a1ab68/gks178f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b242/3367206/865a75002e6a/gks178f5a.jpg

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Drosophila histone H2A variant (H2Av) controls poly(ADP-ribose) polymerase 1 (PARP1) activation in chromatin.
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