JMJD6 is a histone arginine demethylase

被引：493

作者：

Chang, Bingsheng ^{[1
]}

Chen, Yue ^{[1
]}

Zhao, Yingming ^{[1
]}

Bruick, Richard K. ^{[1
]}

机构：

[1] Univ Texas, SW Med Ctr, Dept Biochem, Dallas, TX 75390 USA

来源：

SCIENCE | 2007年 / 318卷 / 5849期

关键词：

D O I：

10.1126/science.1145801

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：

Arginine methylation occurs on a number of proteins involved in a variety of cellular functions. Histone tails are known to be mono- and dimethylated on multiple arginine residues where they influence chromatin remodeling and gene expression. To date, no enzyme has been shown to reverse these regulatory modifications. We demonstrate that the Jumonji domain-containing 6 protein (JMJD6) is a JmjC-containing iron- and 2-oxoglutarate-dependent dioxygenase that demethylates histone H3 at arginine 2 (H3R2) and histone H4 at arginine 3 (H4R3) in both biochemical and cell-based assays. These findings may help explain the many developmental defects observed in the JMJD6(-/-) knockout mice.

引用

页码：444 / 447

页数：4

共 28 条

[1] Histone methylation: Dynamic or static? [J].

Bannister, AJ ;

Schneider, R ;

Kouzarides, T .

CELL, 2002, 109 (07) :801-806

[2]

Bose Jens, 2004, J Biol, V3, P15, DOI 10.1186/jbiol10

[3] Structural insights into histone demethylation by JMJD2 family members [J].

Chen, Zhongzhou ;

Zang, Jianye ;

Whetstine, Johnathan ;

Hong, Xia ;

Davrazou, Foteini ;

Kutateladze, Tatiana G. ;

Simpson, Michael ;

Mao, Qilong ;

Pan, Cheol-Ho ;

Dai, Shaodong ;

Hagman, James ;

Hansen, Kirk ;

Shi, Yang ;

Zhang, Gongyi .

CELL, 2006, 125 (04) :691-702

[4] RBP2 belongs to a family of demethylases, specific for tri- and dimethylated lysine 4 on histone 3 [J].

Christensen, Jesper ;

Agger, Karl ;

Cloos, Paul A. C. ;

Pasini, Diego ;

Rose, Simon ;

Sennels, Lau ;

Rappsilber, Juri ;

Hansen, Klaus H. ;

Salcini, Anna Elisabetta ;

Helin, Kristian .

CELL, 2007, 128 (06) :1063-1076

[5] The phosphatidylserine receptor from Hydra is a nuclear protein with potential Fe(II) dependent oxygenase activity -: art. no. 26 [J].

Cikala, M ;

Alexandrova, O ;

David, CN ;

Pröschel, M ;

Stiening, B ;

Cramer, P ;

Böttger, A .

BMC CELL BIOLOGY, 2004, 5 (1)

[6] Structural studies on 2-oxoglutarate oxygenases and related double-stranded β-helix fold proteins [J].

Clifton, Ian J. ;

McDonough, Michael A. ;

Ehrismann, Dominic ;

Kershaw, Nadia J. ;

Granatino, Nicolas ;

Schofield, Christopher J. .

JOURNAL OF INORGANIC BIOCHEMISTRY, 2006, 100 (04) :644-669

[7] Nuclear localization of the phosphatidylserine receptor protein via multiple nuclear localization signals [J].

Cui, P ;

Qin, BM ;

Liu, N ;

Pan, GJ ;

Pei, DQ .

EXPERIMENTAL CELL RESEARCH, 2004, 293 (01) :154-163

[8] Histone deimination antagonizes arginine methylation [J].

Cuthbert, GL ;

Daujat, S ;

Snowden, AW ;

Erdjument-Bromage, H ;

Hagiwara, T ;

Yamada, M ;

Schneider, R ;

Gregory, PD ;

Tempst, P ;

Bannister, AJ ;

Kouzarides, T .

CELL, 2004, 118 (05) :545-553

[9] Structure of factor-inhibiting hypoxia-inducible factor 1: An asparaginyl hydroxylase involved in the hypoxic response pathway [J].

Dann, CE ;

Bruick, RK ;

Deisenhofer, J .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (24) :15351-15356

[10] Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1α [J].

Elkins, JM ;

Hewitson, KS ;

McNeill, LA ;

Seibel, JF ;

Schlemminger, I ;

Pugh, CW ;

Ratcliffe, PJ ;

Schofield, CJ .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (03) :1802-1806

← 1 2 3 →