Solution Structure of MSL2 CXC Domain Reveals an Unusual Zn(3)Cys(9) Cluster and Similarity to Pre-SET Domains of Histone Lysine Methyltransferases

doi:10.1371/journal.pone.0045437

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	Solution Structure of MSL2 CXC Domain Reveals an Unusual Zn(3)Cys(9) Cluster and Similarity to Pre-SET Domains of Histone Lysine Methyltransferases
	Zheng, Sanduo 3,4; Wang, Jia 3,4; Feng, Yingang1,2 ; Wang, Jinfeng 2; Ye, Keqiong 4
	2012-09-20
发表期刊	PLOS ONE
卷号	7 期号:9
摘要	The dosage compensation complex (DCC) binds to single X chromosomes in Drosophila males and increases the transcription level of X-linked genes by approximately twofold. Male-specific lethal 2 (MSL2) together with MSL1 mediates the initial recruitment of the DCC to high-affinity sites in the X chromosome. MSL2 contains a DNA-binding cysteine-rich CXC domain that is important for X targeting. In this study, we determined the solution structure of MSL2 CXC domain by NMR spectroscopy. We identified three zinc ions in the CXC domain and determined the metal-to-cysteine connectivities from H-1-Cd-113 correlation experiments. The structure reveals an unusual zinc-cysteine cluster composed of three zinc ions coordinated by six terminal and three bridging cysteines. The CXC domain exhibits unexpected structural homology to pre-SET motifs of histone lysine methyltransferases, expanding the distribution and structural diversity of the CXC domain superfamily. Our findings provide novel structural insight into the evolution and function of CXC domains.
文章类型	Article
WOS标题词	Science & Technology
DOI	10.1371/journal.pone.0045437
关键词[WOS]	DOSAGE COMPENSATION COMPLEX ; MALE-SPECIFIC LETHAL-2 ; DNA-BINDING PROTEIN ; X-CHROMOSOME ; RING FINGER ; MACROMOLECULAR STRUCTURE ; DROSOPHILA-MELANOGASTER ; NMR STRUCTURE ; GENE ; METALLOTHIONEIN
收录类别	SCI
语种	英语
WOS研究方向	Science & Technology - Other Topics
WOS类目	Multidisciplinary Sciences
WOS记录号	WOS:000309388900053
引用统计
文献类型	期刊论文
条目标识符	http://ir.qibebt.ac.cn/handle/337004/6065
专题	代谢物组学研究组
作者单位	1.Chinese Acad Sci, Shandong Prov Key Lab Energy Genet, Qingdao Inst BioEnergy & Bioproc Technol, Qingdao, Shangdong, Peoples R China 2.Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100080, Peoples R China 3.Beijing Normal Univ, Dept Biochem & Mol Biol, Coll Life Sci, Beijing 100875, Peoples R China 4.Natl Inst Biol Sci, Beijing, Peoples R China
推荐引用方式 GB/T 7714	Zheng, Sanduo,Wang, Jia,Feng, Yingang,et al. Solution Structure of MSL2 CXC Domain Reveals an Unusual Zn(3)Cys(9) Cluster and Similarity to Pre-SET Domains of Histone Lysine Methyltransferases[J]. PLOS ONE,2012,7(9).
APA	Zheng, Sanduo,Wang, Jia,Feng, Yingang,Wang, Jinfeng,&Ye, Keqiong.(2012).Solution Structure of MSL2 CXC Domain Reveals an Unusual Zn(3)Cys(9) Cluster and Similarity to Pre-SET Domains of Histone Lysine Methyltransferases.PLOS ONE,7(9).
MLA	Zheng, Sanduo,et al."Solution Structure of MSL2 CXC Domain Reveals an Unusual Zn(3)Cys(9) Cluster and Similarity to Pre-SET Domains of Histone Lysine Methyltransferases".PLOS ONE 7.9(2012).