Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity

Nature

Volumn 448, Issue 7149, 2007, Pages 87-91

  Ng, Stanley S ^a   Kavanagh, Kathryn L ^a   McDonough, Michael A ^b   Butler, Danica ^b   Pilka, Ewa S ^a   Lienard, Benoit M R ^b   Bray, James E ^a   Savitsky, Pavel ^a   Gileadi, Opher ^a   Von Delft, Frank ^a   Rose, Nathan R ^b   Offer, John ^a   Scheinost, Johanna C ^a   Borowski, Tomasz ^c   Sundstrom, Michael ^a   Schofield, Christopher J ^b   Oppermann, Udo ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c INSTITUTE OF CATALYSIS AND SURFACE CHEMISTRY   (Poland)

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE DEACETYLASE; JUMONJI DOMAIN 2A; UNCLASSIFIED DRUG; ZINC;

CHROMOSOME; CRYSTAL STRUCTURE; DNA; DRUG; GENE EXPRESSION; GENETIC MARKER; GENOME; METHYLATION; PROTEIN; SUBSTRATE;

ARTICLE; BINDING SITE; CONFORMATION; CRYSTAL STRUCTURE; ENZYME SPECIFICITY; METHYLATION; PRIORITY JOURNAL;

EID: 34447133035     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature05971     Document Type: Article

References (17)

1. Margueron, R., Trojer, P. & Reinberg, D. The key to development: interpreting the histone code? Curr. Opin. Genet. Dev. 15, 163-176 (2005).
2. Zhang, Y. & Reinberg, D. Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails. Genes Dev. 15, 2343-2360 (2001).
3. Martin, C. & Zhang, Y. The diverse functions of histone lysine methylation. Nature Rev. Mol. Cell Biol. 6, 838-849 (2005).
4. Shi, Y. et al. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119, 941-953 (2004).
5. Tsukada, Y. et al. Histone demethylation by a family of JmjC domain-containing proteins. Nature 439, 811-816 (2006).
6. Klose, R. J., Kallin, E. M. & Zhang, Y. JmjC-domain-containing proteins and histone demethylation. Nature Rev. Genet. 7, 715-727 (2006).
7. Whetstine, J. R. et al. Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases. Cell 125, 467-481 (2006).
8. Flashman, E. & Schofield, C. J. The most versatile of all reactive intermediates? Nature Chem. Biol. 3, 86-87 (2007).
9. Chen, Z. et al. Structural insights into histone demethylation by JMJD2 family members. Cell 125, 691-702 (2006).
10. Clifton, I. J. et al. Structural studies on 2-oxoglutarate oxygenases and related double-stranded β-helix fold proteins. J. Inorg. Biochem. 100, 644-669 (2006).
11. Lo, W. S. et al. Snf1-a histone kinase that works in concert with the histone acetyltransferase Gcn5 to regulate transcription. Science 293, 1142-1146 (2001).
12. Nelson, C. J., Santos-Rosa, H. & Kouzarides, T. Proline isomerization of histone H3 regulates lysine methylation and gene expression. Cell 126, 905-916 (2006).
13. Price, J. C., Barr, E. W., Tirupati, B., Bollinger, J. M. & Krebs, C. Kinetic dissection of the catalytic mechanism of taurine:α-ketoglutarate dioxygenase (TauD) from Escherichia coli. Biochemistry 42, 7497-7508 (2003).
14. Grzyska, P. K. et al. Steady-state and transient kinetic analyses of taurine/α-ketoglutarate dioxygenase: effects of oxygen concentration, alternative sulfonates, and active-site variants on the FeIV-oxo intermediate. Biochemistry 44, 3845-3855 (2005).
15. Elkins, J. M. et al. Structure of Factor-inhibiting Hypoxia-inducible Factor (HIF) reveals mechanism of oxidative modification of HIF-1. J. Biol. Chem. 278, 1802-1806 (2003).
16. Liang, G., Klose, R. J., Gardner, K. E. & Zhang, Y. Yeast Jhd2p is a histone H3 Lys4 trimethyl demethylase. Nature Struct. Mol. Biol. 14, 243-245 (2007).
17. Seward, D. J. et al. Demethylation of trimethylated histone H3 Lys4 in vivo by JARID1 JmjC proteins. Nature Struct. Mol. Biol. 14, 240-242 (2007).