中文摘要：

溴区包含蛋白7（BRD7）是采用cDNA代表性差异分析方法克隆的一个新基因．研究证实了BRD7能够与乙酰化的组蛋白3结合，其识别位点在组蛋白3的14位氨基酸；并且证实了溴区结构域（Bromodomain）缺失型的BRD7突变体失去了与乙酰化组蛋白3的结合能力．Bromodomain是在进化上高度保守的功能结构域，该结构域在空间构象上具有鲜明的特征：包括4个左手、呈反向平行排列的“螺旋（α2，αA，αB,αc）”以及2个“连结环”（ZA loop，BC loop）．通过生物信息学等综合分析，预测BRD7可能具有上述特征．依据上述分析结果，构建了BRD7的Bromodomain相关缺失突变体，通过肽段结合实验分析上述突变体与乙酰化组蛋白3结合的能力．结果表明，ZA loop与BC loop的完整性对于BRD7结合乙酰化的组蛋白3有着重要的意义．同时通过免疫荧光分析，证实了ZA loop与BC loop的完整性能够影响BRD7的亚细胞定位．最后，证实了BRD7与CBP可能存在交互作用．CBP不仅具有乙酰化转移酶活性（HATs），能够对组蛋白末端进行乙酰化修饰，并且作为一种重要的细胞转录因子广泛参与细胞的各种生物学活动．

英文摘要：

BRD7, a novel NPC-related gene, was isolated through cDNA representational difference analysis （RDA）. The studies showed that wild-type BRD7 interacted with H3 peptide acetylated at Lys14, while the bromodomain deleted mutant lost this ability. Bromodomain is an evolutionally conserved domain which forms a bundle of four a-helices（αz, αA, αB, αC） and two loops （ZA loop, BC loop）. Alignment of the amino acid sequence of BRD7 protein with known structure of proteins in PDB （protein database）, it was considered that Bromodomain of BRD7 has the same characteristic. Based on results of bio-informatics, mutants of Bromodomain were constructed. The peptide binding assays was performed to detect the binding of mutants with acetylated histone H3. The results indicated that two loops （ZA loop, BC loop） were essential for Bromodomain binding to acetylated histone H3, while two loops（ZA loop, BC loop） could influence the sub-cellular location of BRD7 through indirect immunofluorescence. At last, it was found that the CBP （CREB binding protein） is a novel interaction protein of BRDT. The CBP not only has histone acetyltransferases （HATs） to acetylate lysines on N-terminal tails of histones but also plays a key role as co-activator for a wide variety of transcription factors.