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Molecular Basis of the Interaction of Saccharomyces cerevisiae Eaf3 Chromo Domain with Methylated H3K36

文献类型：期刊论文

作者Sun, Bingfa1,3; Hong, Jing2; Zhang, Peng1,3; Dong, Xianchi1,3,4; Shen, Xu2; Lin, Donghai2; Ding, Jianping1,3
刊名JOURNAL OF BIOLOGICAL CHEMISTRY
出版日期2008-12-26
卷号283期号:52页码:36504-36512
ISSN号0021-9258
DOI10.1074/jbc.M806564200
文献子类Article
英文摘要Eaf3 is a component of both NuA4 histone acetyltransferase and Rpd3S histone deacetylase complexes in Saccharomyces cerevisiae. It is involved in the regulation of the global pattern of histone acetylation that distinguishes promoters from coding regions. Eaf3 contains a chromo domain at the N terminus that can bind to methylated Lys-36 of histone H3 (H3K36). We report here the crystal structures of the Eaf3 chromo domain in two truncation forms. Unlike the typical HP1 and Polycomb chromo domains, which contain a large groove to bind the modified histone tail, the Eaf3 chromo domain assumes an autoinhibited chromo barrel domain similar to the human MRG15 chromo domain. Compared with other chromo domains, the Eaf3 chromo domain contains a unique 38-residue insertion that folds into two short beta-strands and a long flexible loop to flank the beta-barrel core. Both isothermal titration calorimetry and surface plasmon resonance studies indicate that the interaction between the Eaf3 chromo domain and the trimethylated H3K36 peptide is relatively weak, with a K-D of similar to 10(-4) M. NMR titration studies demonstrate that the methylated H3K36 peptide is bound to the cleft formed by the C-terminal alpha-helix and the beta-barrel core. Site-directed mutagenesis study and in vitro binding assay results show that the conserved aromatic residues Tyr-23, Tyr-81, Trp-84, and Trp-88, which form a hydrophobic pocket at one end of the beta-barrel, are essential for the binding of the methylated H3K36. These results reveal the molecular mechanism of the recognition and binding of the methylated H3K36 by Eaf3 and provide new insights into the functional roles of the Eaf3 chromo domain.
WOS关键词DOSAGE COMPENSATION COMPLEX ; HISTONE H3 TAIL ; FUNCTIONAL-INTEGRATION ; STRUCTURAL BASIS ; BINDING MODULES ; MSL COMPLEX ; LYSINE 9 ; TRANSCRIPTION ; ACETYLATION ; PROTEIN
资助项目Ministry of Science and Technology of China[2006CB806501] ; Ministry of Science and Technology of China[2006AA02Z112] ; Ministry of Science and Technology of China[2006AA02A313] ; Ministry of Science and Technology of China[2007CB914302] ; Ministry of Science and Technology of China[2007CB914304] ; National Natural Science Foundation of China[30570379] ; National Natural Science Foundation of China[30570352] ; National Natural Science Foundation of China[30623002] ; National Natural Science Foundation of China[30730028] ; Chinese Academy of Sciences[KSCX2-YW-R-107] ; Chinese Academy of Sciences[KSCX2-YW-R-104] ; Science and Technology Commission of Shanghai Municipality[07XD14032] ; Science and Technology Commission of Shanghai Municipality[07DZ22009]
WOS研究方向Biochemistry & Molecular Biology
语种英语
出版者AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
WOS记录号WOS:000261840500048
源URL[http://119.78.100.183/handle/2S10ELR8/279404]  
专题分析化学研究室
通讯作者Lin, Donghai
作者单位1.Chinese Acad Sci, State Key Lab Mol Biol, Shanghai 201203, Peoples R China;
2.Chinese Acad Sci, Shanghai Inst Mat Med, Shanghai 201203, Peoples R China;
3.Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, Res Ctr Struct Biol, Shanghai 201203, Peoples R China;
4.Chinese Acad Sci, Grad Sch, Shanghai 200031, Peoples R China
推荐引用方式
GB/T 7714		 Sun, Bingfa,Hong, Jing,Zhang, Peng,et al. Molecular Basis of the Interaction of Saccharomyces cerevisiae Eaf3 Chromo Domain with Methylated H3K36[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2008,283(52):36504-36512.
APA Sun, Bingfa.,Hong, Jing.,Zhang, Peng.,Dong, Xianchi.,Shen, Xu.,...&Ding, Jianping.(2008).Molecular Basis of the Interaction of Saccharomyces cerevisiae Eaf3 Chromo Domain with Methylated H3K36.JOURNAL OF BIOLOGICAL CHEMISTRY,283(52),36504-36512.
MLA Sun, Bingfa,et al."Molecular Basis of the Interaction of Saccharomyces cerevisiae Eaf3 Chromo Domain with Methylated H3K36".JOURNAL OF BIOLOGICAL CHEMISTRY 283.52(2008):36504-36512.

入库方式： OAI收割

来源：上海药物研究所

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