Open AccessInteraction of JMJD6 with single-stranded RNA
Author(s) -
Xue-Ren Hong,
Jianye Zang,
Janicé White,
Chao Wang,
CheolHo Pan,
Rui Zhao,
Robert C. Murphy,
Shaodong Dai,
Peter M. Henson,
John W. Kappler,
James Hagman,
Gongyi Zhang
Publication year - 2010
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.1008832107
Subject(s) - rna , demethylase , dna , chemistry , histone , stereochemistry , biochemistry , biophysics , crystallography , biology , gene
JMJD6 is a Jumonji C domain-containing hydroxylase. JMJD6 binds α-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 α-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.