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多结构域 C2H2 锌指蛋白 CTCF 的绝缘子功能：必要性与充分性。

The insulator functions of the polydactyl C2H2 zinc finger protein CTCF: Necessity versus sufficiency.

机构信息

Department of the Control of Genetic Processes, Institute of Gene Biology Russian Academy of Sciences, 34/5 Vavilov St., Moscow 119334, Russia.

Center for Precision Genome Editing and Genetic Technologies for Biomedicine, Institute of Gene Biology, Russian Academy of Sciences, 34/5 Vavilov St., Moscow 119334, Russia.

出版信息

Sci Adv. 2020 Mar 25;6(13):eaaz3152. doi: 10.1126/sciadv.aaz3152. eCollection 2020 Mar.

DOI:10.1126/sciadv.aaz3152
PMID:32232161
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7096168/
Abstract

In mammals, a C2H2 zinc finger (C2H2) protein, CTCF, acts as the master regulator of chromosomal architecture and of the expression of Hox gene clusters. Like mammalian CTCF, the homolog, dCTCF, localizes to boundaries in the bithorax complex (BX-C). Here, we have determined the minimal requirements for the assembly of a functional boundary by dCTCF and two other C2H2 zinc finger proteins, Pita and Su(Hw). Although binding sites for these proteins are essential for the insulator activity of BX-C boundaries, these binding sites alone are insufficient to create a functional boundary. dCTCF cannot effectively bind to a single recognition sequence in chromatin or generate a functional insulator without the help of additional proteins. In addition, for boundary elements in BX-C at least four binding sites for dCTCF or the presence of additional DNA binding factors is required to generate a functional insulator.

摘要

在哺乳动物中，一种 C2H2 锌指（C2H2）蛋白 CTCF 作为染色体结构和 Hox 基因簇表达的主要调节剂。与哺乳动物 CTCF 一样，同源物 dCTCF 定位于双胸复合体 (BX-C) 的边界处。在这里，我们确定了 dCTCF 以及另外两种 C2H2 锌指蛋白 Pita 和 Su(Hw) 组装功能性边界的最小要求。尽管这些蛋白质的结合位点对于 BX-C 边界的绝缘子活性是必需的，但这些结合位点本身不足以创建功能性边界。dCTCF 不能有效地在染色质中结合单个识别序列，也不能在没有其他蛋白质帮助的情况下产生功能性绝缘子。此外，对于 BX-C 中的边界元件，至少需要四个 dCTCF 或其他 DNA 结合因子的结合位点才能产生功能性绝缘子。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7490/7096168/d60c944e53c3/aaz3152-F6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7490/7096168/b2a997f65663/aaz3152-F1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7490/7096168/940d6b53b405/aaz3152-F2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7490/7096168/99b9bf4b2cca/aaz3152-F3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7490/7096168/9ed82eb7abb8/aaz3152-F4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7490/7096168/ea6b9dfa3b77/aaz3152-F5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7490/7096168/d60c944e53c3/aaz3152-F6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7490/7096168/b2a997f65663/aaz3152-F1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7490/7096168/940d6b53b405/aaz3152-F2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7490/7096168/99b9bf4b2cca/aaz3152-F3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7490/7096168/9ed82eb7abb8/aaz3152-F4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7490/7096168/ea6b9dfa3b77/aaz3152-F5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7490/7096168/d60c944e53c3/aaz3152-F6.jpg

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