The p23 molecular chaperone and GCN5 acetylase jointly modulate protein-DNA dynamics and open chromatin status.
The p23 molecular chaperone and GCN5 acetylase jointly modulate protein-DNA dynamics and open chromatin status.
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DOI：
10.1016/j.molcel.2012.08.026
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发表时间：
2012-11-09
期刊：
影响因子：
16
通讯作者：
Freeman, Brian C.
中科院分区：
文献类型：
--
作者：
Zelin, Elena;Zhang, Yang;Toogun, Oyetunji A.;Zhong, Sheng;Freeman, Brian C.
细胞过程通过多步骤途径发挥作用，这些途径依赖于顺序蛋白复合物的控制结合和解离。虽然动态作用对繁殖和终止工作至关重要，但用于分解生物结构的机制尚未完全了解。在这里，我们发现p23分子伴侣启动蛋白质- dna复合物的分解，而GCN5乙酰转移酶通过赖氨酸乙酰化延长了解离状态。通过调节DNA结合状态，我们发现p23和GCN5的保守和必要的联合活性影响转录因子的激活电位和对环境线索的响应时间。值得注意的是，p23和GCN5需要维持沿基因组开放的染色质区域，这表明动态蛋白质行为是各种dna相关事件的关键特征。我们的数据支持p23和GCN5通过控制蛋白质- dna复合物的寿命来调节多种多步骤途径的模型。
Cellular processes function through multi-step pathways that are reliant on the controlled association and disassociation of sequential protein complexes. While dynamic action is critical to propagate and terminate work, the mechanisms used to disassemble biological structures are not fully understood. Here, we show that the p23 molecular chaperone initiates disassembly of protein-DNA complexes and that the GCN5 acetyltransferase prolongs the dissociated state through lysine acetylation. By modulating the DNA bound-state, we found that the conserved and essential joint activities of p23 and GCN5 impacted transcription factor activation potential and response time to an environmental cue. Notably, p23 and GCN5 were required to maintain open chromatin regions along the genome indicating that dynamic protein behavior is a critical feature of various DNA-associated events. Our data support a model in which p23 and GCN5 regulate diverse multi-step pathways by controlling the longevity of protein-DNA complexes.
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