Interaction of JMJD6 with single-stranded RNA

被引:88
作者
Hong, Xia [1 ]
Zang, Jianye [2 ]
White, Janice [3 ]
Wang, Chao [1 ]
Pan, Cheol-Ho [4 ]
Zhao, Rui [5 ]
Murphy, Robert C. [6 ]
Dai, Shaodong [1 ]
Henson, Peter [1 ,7 ]
Kappler, John W. [1 ,3 ]
Hagman, James [1 ,5 ]
Zhang, Gongyi [1 ]
机构
[1] Natl Jewish Hlth, Integrated Dept Immunol, Denver, CO 80206 USA
[2] Univ Sci & Technol China, Sch Life Sci, Hefei 230026, Peoples R China
[3] Natl Jewish Hlth, Howard Hughes Med Inst, Denver, CO 80206 USA
[4] Gangneung Inst, Korea Inst Sci & Technol, Nat Prod Res Ctr, Kangnung, South Korea
[5] Univ Colorado, Sch Med, Dept Biochem & Mol Genet, Aurora, CO 80045 USA
[6] Univ Colorado, Sch Med, Dept Pharmacol, Aurora, CO 80045 USA
[7] Natl Jewish Hlth, Dept Pediat, Denver, CO 80206 USA
基金
美国国家卫生研究院;
关键词
RNA binding proteins; RNA modification; RNA splicing; PHOSPHATIDYLSERINE RECEPTOR; OXIDATIVE DEMETHYLATION; HISTONE DEMETHYLATION; CRYSTAL-STRUCTURES; STRUCTURAL BASIS; NUCLEAR; PROTEIN; FAMILY; ENGULFMENT; MECHANISM;
D O I
10.1073/pnas.1008832107
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
JMJD6 is a Jumonji C domain-containing hydroxylase. JMJD6 binds alpha-ketoglutarate and iron and has been characterized as either a histone arginine demethylase or U2AF65 lysyl hydroxylase. Here, we describe the structures of JMJD6 with and without alpha-keto-glutarate, which revealed a novel substrate binding groove and two positively charged surfaces. The structures also contain a stack of aromatic residues located near the active center. The side chain of one residue within this stack assumed different conformations in the two structures. Interestingly, JMJD6 bound efficiently to single-stranded RNA, but not to single-stranded DNA, double-stranded RNA, or double-stranded DNA. These structural features and truncation analysis of JMJD6 suggest that JMJD6 may bind and modify single-stand RNA rather than the previously reported peptide substrates.
引用
收藏
页码:14568 / 14572
页数:5
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