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Ring1B对于胚胎细胞中发育控制基因和PRC1蛋白的调控至关重要，但对于X染色体失活并非如此。

Ring1B is crucial for the regulation of developmental control genes and PRC1 proteins but not X inactivation in embryonic cells.

作者信息

Leeb Martin, Wutz Anton

机构信息

Research Institute of Molecular Pathology, Vienna, Austria.

出版信息

J Cell Biol. 2007 Jul 16;178(2):219-29. doi: 10.1083/jcb.200612127. Epub 2007 Jul 9.

DOI:10.1083/jcb.200612127
PMID:17620408
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2064442/
Abstract

The Polycomb group (PcG) gene Ring1B has been implicated in the repression of developmental control genes and X inactivation and is essential for embryogenesis. Ring1B protein contains a RING finger domain and functions as an E3 ubiquitin ligase that is crucial for the monoubiquitination of histone H2A (H2AK119ub1). Here, we study the function of Ring1B in mouse embryonic stem (ES) cells. The deletion of Ring1B causes the loss of several PcG proteins, showing an unanticipated function in the regulation of PcG protein levels. Derepression of lineage genes and an aberrant differentiation potential is observed in Ring1B-deficient ES cells. Despite a crucial function of Ring1B in establishing the chromosome-wide ubiquitination of histone H2A lysine 119 (H2AK119ub1) upon Xist expression in ES cells, the initiation of silencing by Xist is independent of Ring1B. Other chromatin marks associated with the initiation of X inactivation are not affected in Ring1B-deficient cells, suggesting compensation for the loss of Ring1B in X inactivation in contrast to the repression of lineage genes.

摘要

多梳蛋白家族（PcG）基因Ring1B与发育控制基因的抑制及X染色体失活有关，对胚胎发育至关重要。Ring1B蛋白含有一个环状结构域，作为E3泛素连接酶发挥作用，这对组蛋白H2A的单泛素化（H2AK119ub1）至关重要。在此，我们研究Ring1B在小鼠胚胎干细胞（ES细胞）中的功能。Ring1B的缺失导致几种PcG蛋白丢失，表明其在调控PcG蛋白水平方面具有意想不到的功能。在Ring1B缺陷的ES细胞中观察到谱系基因的去抑制和异常的分化潜能。尽管Ring1B在ES细胞中Xist表达时建立全染色体范围的组蛋白H2A赖氨酸119泛素化（H2AK119ub1）方面具有关键作用，但Xist介导的沉默起始独立于Ring1B。与X染色体失活起始相关的其他染色质标记在Ring1B缺陷细胞中不受影响，这表明与谱系基因的抑制相反，在X染色体失活过程中存在对Ring1B缺失的补偿机制。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb1d/2064442/303f1aa1258b/jcb1780219f05.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb1d/2064442/a6fc1696b4eb/jcb1780219f01.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb1d/2064442/86e2b3e8f48d/jcb1780219f02.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb1d/2064442/096d1bb321bf/jcb1780219f03.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb1d/2064442/642f5780e01b/jcb1780219f04.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb1d/2064442/303f1aa1258b/jcb1780219f05.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb1d/2064442/a6fc1696b4eb/jcb1780219f01.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb1d/2064442/86e2b3e8f48d/jcb1780219f02.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb1d/2064442/096d1bb321bf/jcb1780219f03.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb1d/2064442/642f5780e01b/jcb1780219f04.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb1d/2064442/303f1aa1258b/jcb1780219f05.jpg

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