Interaction of JMJD6 with single-stranded RNA

Title
Interaction of JMJD6 with single-stranded RNA
Authors
Xia HongJianye ZangJanice WhiteChao Wang판철호Rui ZhaoRobert C. MurphyShaodong DaiPeter HensonJohn W. KapplerJames HagmanGongyi Zhang
Keywords
JMJD6; Jumonji C domain-containing hydroxylase; RNA binding proteins; single-stranded RNA; 3D structure; RNA modification; RNA splicing
Issue Date
2010-08
Publisher
Proceedings of the National Academy of Sciences of the United States of America
Citation
VOL 107, NO 33, 14568-14572
Abstract
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, doublestranded 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.
URI
http://pubs.kist.re.kr/handle/201004/37852
ISSN
0027-8424
Appears in Collections:
KIST Publication > Article
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