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

	Molecular Basis of the Interaction of Saccharomyces cerevisiae Eaf3 Chromo Domain with Methylated H3K36
	Sun, BF; Hong, J; Zhang, P; Dong, XC; Shen, X; Lin, DH; Ding, JP
刊名	JOURNAL OF BIOLOGICAL CHEMISTRY
	2008
卷号	283 期号:52 页码:36504-36512
通讯作者	Lin, DH (reprint author), Chinese Acad Sci, Shanghai Inst Mat Med, 555 Zu Chong Zhi Rd, Shanghai 201203, Peoples R China.,dhlin@mail.shcnc.ac.cn ; jpding@sibs.ac.cn
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.
学科主题	Biochemistry & Molecular Biology
类目[WOS]	Biochemistry & Molecular Biology
关键词[WOS]	DOSAGE COMPENSATION COMPLEX ; HISTONE H3 TAIL ; FUNCTIONAL-INTEGRATION ; STRUCTURAL BASIS ; BINDING MODULES ; MSL COMPLEX ; LYSINE 9 ; TRANSCRIPTION ; ACETYLATION ; PROTEIN
收录类别	SCI
语种	英语
WOS记录号	WOS:000261840500048
内容类型	期刊论文
版本	出版稿
源URL	[http://202.127.25.143/handle/331003/1482]
专题	上海生化细胞研究所_上海生科院生化细胞研究所
推荐引用方式 GB/T 7714	Sun, BF,Hong, J,Zhang, P,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, BF.,Hong, J.,Zhang, P.,Dong, XC.,Shen, X.,...&Ding, JP.(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, BF,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.