Acetylation of p65 at lysine 314 is important for late NF-kappaB-dependent gene expression.
Acetylation of p65 at lysine 314 is important for late NF-kappaB-dependent gene expression.
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DOI：
10.1186/1471-2164-11-22
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发表时间：
2010-01-11
期刊：
影响因子：
4.4
通讯作者：
Hottiger MO
中科院分区：
文献类型：
--
作者：
Rothgiesser KM;Fey M;Hottiger MO
NF-κB调节大量参与免疫和炎症反应、凋亡、细胞增殖、分化和存活的靶基因的表达。我们先前报道了NF-κB亚基p65在体外和体内被组蛋白乙酰转移酶p300在三个不同的赖氨酸（K310、K314和K315）乙酰化。在这项研究中，我们描述了p65在赖氨酸314和315处的位点特异性突变增强了NF-κB靶基因亚组的基因表达，包括Mmp 10和Mmp 13。主要在TNFα刺激后3小时观察到基因表达增加。染色质免疫沉淀（ChIP）实验与乙酰化赖氨酸314提出的抗体显示，染色质结合p65确实是乙酰化赖氨酸314。总之，我们的研究结果确定K314的乙酰化是p65的重要调节修饰，随后是NF-κ B依赖性基因表达。
NF-κB regulates the expression of a large number of target genes involved in the immune and inflammatory response, apoptosis, cell proliferation, differentiation and survival. We have earlier reported that p65, a subunit of NF-κB, is acetylated in vitro and in vivo at three different lysines (K310, K314 and K315) by the histone acetyltransferase p300. In this study, we describe that site-specific mutation of p65 at lysines 314 and 315 enhances gene expression of a subset of NF-κB target genes including Mmp10 and Mmp13. Increased gene expression was mainly observed three hours after TNFα stimulation. Chromatin immunoprecipitation (ChIP) experiments with an antibody raised against acetylated lysine 314 revealed that chromatin-bound p65 is indeed acetylated at lysine 314. Together, our results establish acetylation of K314 as an important regulatory modification of p65 and subsequently of NF-κB-dependent gene expression.
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