Regulation of histone acetylation and nucleosome assembly by transcription factor JDP2
Regulation of histone acetylation and nucleosome assembly by transcription factor JDP2
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DOI：
10.1038/nsmb1063
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发表时间：
2006-04-01
影响因子：
16.8
通讯作者：
Yokoyama, KK
中科院分区：
文献类型：
--
作者：
Jin, CY;Kato, K;Yokoyama, KK
Jun二聚化蛋白-2（JDP 2）是AP-1转录因子的一个组分，其抑制由Jun蛋白家族介导的反式激活。在这里，我们研究了JDP 2的功能机制，并表明它可以抑制p300介导的核心组蛋白在体外和体内的乙酰化。组蛋白乙酰化的抑制需要JDP 2的N-末端35个残基和DNA结合区。此外，我们证明了JDP 2在体外具有组蛋白伴侣活性。这些结果表明，序列特异性DNA结合蛋白JDP 2可能通过直接调节组蛋白的修饰和染色质的组装来控制转录。
Jun dimerization protein-2 ( JDP2) is a component of the AP-1 transcription factor that represses transactivation mediated by the Jun family of proteins. Here, we examine the functional mechanisms of JDP2 and show that it can inhibit p300-mediated acetylation of core histones in vitro and in vivo. Inhibition of histone acetylation requires the N-terminal 35 residues and the DNA-binding region of JDP2. In addition, we demonstrate that JDP2 has histone-chaperone activity in vitro. These results suggest that the sequence-specific DNA-binding protein JDP2 may control transcription via direct regulation of the modification of histones and the assembly of chromatin.