JMJD6 与单链 RNA 的相互作用。
Interaction of JMJD6 with single-stranded RNA.
机构信息
Integrated Department of Immunology, National Jewish Health, Denver, CO 80206.
出版信息
Proc Natl Acad Sci U S A. 2010 Aug 17;107(33):14568-72. doi: 10.1073/pnas.1008832107. Epub 2010 Aug 2.
Abstract
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-ketoglutarate, 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.
摘要
JMJD6 是一种含有 Jumonji C 结构域的羟化酶。JMJD6 结合α-酮戊二酸和铁，被鉴定为组蛋白精氨酸去甲基酶或 U2AF65 赖氨酸羟化酶。在这里，我们描述了含有和不含有α-酮戊二酸的 JMJD6 的结构，揭示了一个新的底物结合槽和两个带正电荷的表面。这些结构还包含一个位于活性中心附近的芳香族残基堆叠。该堆叠中的一个残基的侧链在这两个结构中呈现出不同的构象。有趣的是，JMJD6 能够有效地结合单链 RNA，但不能结合单链 DNA、双链 RNA 或双链 DNA。这些结构特征和 JMJD6 的截断分析表明，JMJD6 可能结合并修饰单链 RNA，而不是之前报道的肽底物。
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