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首页> 外文期刊>Molecular and Cellular Biology >Proteasome Activity Modulates Chromatin Modifications and RNA Polymerase II Phosphorylation To Enhance Glucocorticoid Receptor-Mediated Transcription
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Proteasome Activity Modulates Chromatin Modifications and RNA Polymerase II Phosphorylation To Enhance Glucocorticoid Receptor-Mediated Transcription

机译：蛋白酶体活性调节染色质修饰和RNA聚合酶II磷酸化，以增强糖皮质激素受体介导的转录。

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摘要

The 26S proteasome modulates steroid hormone receptor-dependent gene transcription at least in part by regulating turnover and recycling of receptor/transcriptional DNA complexes, thereby ensuring continued hormone response. For the glucocorticoid receptor (GR), inhibition of proteasome-mediated proteolysis or RNA interference-mediated depletion of specific proteasome subunits results in an increase in gene expression. To facilitate transcription, proteasome inhibition alters at least two features associated with modification of chromatin architecture and gene transcription. First, proteasome inhibition increases trimethyl histone H3K4 levels with a corresponding accumulation of this modification on GR-regulated promoters in vivo. Secondly, global levels of phosphorylated RNA polymerase II (Pol II) increase, together with hormone-dependent association of the phosphorylated Pol II, with the promoter and the body of the activated gene. We propose that apart from modulating receptor turnover, the proteasome directly influences both the transcription machinery and chromatin structure, factors integral to nuclear receptor-regulated gene transcription.
机译：26S蛋白酶体至少部分通过调节受体/转录DNA复合物的更新和循环来调节甾体激素受体依赖性基因的转录，从而确保持续的激素反应。对于糖皮质激素受体（GR），蛋白酶体介导的蛋白水解的抑制或RNA干扰介导的对特定蛋白酶体亚基的消耗的抑制导致基因表达的增加。为了促进转录，蛋白酶体抑制改变了至少两种与染色质结构和基因转录的修饰有关的特征。首先，蛋白酶体抑制增加了三甲基组蛋白H3K4的水平，并在体内GR调节的启动子上相应积累了这种修饰。其次，磷酸化RNA聚合酶II（Pol II）的整体水平增加，并且磷酸化Pol II的激素依赖性缔合与启动子和激活基因的体一起增加。我们提出，除了调节受体转换外，蛋白酶体还直接影响转录机制和染色质结构，这是核受体调节基因转录必不可少的因素。

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