Characterization of a novel WHSC1-associated SET domain protein with H3K4 and H3K27 methyltransferase activity
Characterization of a novel WHSC1-associated SET domain protein with H3K4 and H3K27 methyltransferase activity
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DOI：
10.1016/j.bbrc.2006.04.095
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发表时间：
2006-06-23
影响因子：
3.1
通讯作者：
Seo, Sang Beom
中科院分区：
文献类型：
--
作者：
Kim, Sung Mi;Kee, Hae Jin;Seo, Sang Beom
进化上保守的SET结构域最初在三种果蝇蛋白中鉴定：杂色抑制子（Su（var）3-9）、zeste增强子（E（z））和三胸。已知一些含有SET结构域的蛋白质引起组蛋白赖氨酸残基的甲基化。基于使用生物信息学工具搜索包含SET结构域的蛋白质，我们鉴定并随后命名为WHISTLE的新型SET结构域，其具有历史甲基转移酶（HMTase）活性。为了表征WHISTLE，我们进行了HMTase测定、质谱分析、赖氨酸特异性和转染测定。质谱和免疫印迹分析表明，WHISTLE二甲基化H3 K4和二，三甲基化H3 K27的历史。WHISTLE的过表达抑制了SV 40启动子的转录。我们的研究结果表明，WHISTLE是一个新的SET域包含一个蛋白质具有特异性H3 K4和H3 K27 HMTase活性。(c)2006年爱思唯尔公司All rights reserved.
Evolutionary conserved SET domains were originally identified in three Drosophila proteins: suppressor of variegation (Su (var) 3-9), enhancer of zeste (E(z)), and the trithorax. Some of the SET-domain containing proteins have been known to elicit methylation of histone lysine residues. Based on a search for SET-domain containing proteins using bioinformatic tools, we identified and subsequently named a novel SET domain as WHISTLE, that has historic methyltransferase (HMTase) activity. To characterize WHISTLE, we performed an HMTase assay, mass spectrometric analysis, lysine specificity, and transfection assays. Mass spectrometric and immunoblot analysis revealed that WHISTLE di-methylates H3K4 and di-, and tri-methylates H3K27 of histories. Overexpression of WHISTLE repressed transcription of the SV40 promoter. Our results suggest that WHISTLE is a novel SET domain containing a protein with specific H3K4 and H3K27 HMTase activity. (c) 2006 Elsevier Inc. All rights reserved.