Self-hydroxylation of the splicing factor lysyl hydroxylase, JMJD6

被引：13

作者：

Mantri, Monica ^{[1
]}

Webby, Celia J. ^{[1
]}

Loik, Nikita D. ^{[1
]}

Hamed, Refaat B. ^{[1
,2
]}

Nielsen, Michael L. ^{[3
]}

McDonough, Michael A. ^{[1
]}

McCullagh, James S. O. ^{[1
]}

Boettger, Angelika ^{[4
]}

Schofield, Christopher J. ^{[1
]}

Wolf, Alexander ^{[1
]}

机构：

[1] Chem Res Lab, Oxford OX1 3TA, England

[2] Assiut Univ, Fac Pharm, Dept Pharmacognosy, Assiut 71526, Egypt

[3] Univ Copenhagen, Fac Hlth Sci, Novo Nordisk Fdn, Dept Prote,Ctr Prot Res, DK-2200 Copenhagen, Denmark

[4] Univ Munich, Dept Biol 2, D-82152 Planegg Martinsried, Germany

来源：

MEDCHEMCOMM | 2012年 / 3卷 / 01期

基金：

英国惠康基金; 英国生物技术与生命科学研究理事会;

关键词：

ANKYRIN REPEAT DOMAIN; HYPOXIA-INDUCIBLE FACTOR; ALPHA-KETOGLUTARATE; ASPARAGINYL HYDROXYLATION; CRYSTAL-STRUCTURE; PROTEIN; OXYGENASE; RECEPTOR; 2-OXOGLUTARATE; ASCORBATE;

D O I：

10.1039/c1md00225b

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The lysyl 5S-hydroxylase, JMJD6 acts on proteins involved in RNA splicing. We find that in the absence of substrate JMJD6 catalyses turnover of 2OG to succinate. H-1-NMR analyses demonstrate that consumption of 2OG is coupled to succinate formation. MS analyses reveal that JMJD6 undergoes self-hydroxylation in the presence of Fe(II) and 200 resulting in production of 5S-hydroxylysine residues. JMJD6 in human cells is also found to be hydroxylated. Self-hydroxylation of JMJD6 may play a regulatory role in modulating the hydroxylation status of proteins involved in RNA splicing.

引用

页码：80 / 85

页数：6

共 33 条

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Biochemistry, 1998, 37 (39):
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