Lysyl 5-hydroxylation, a novel histone modification, by jumonji domain containing 6 (JMJD6)

Journal of Biological Chemistry

Volumn 288, Issue 9, 2013, Pages 6053-6062

  Unoki, Motoko ^a,b   Masuda, Akiko ^c   Dohmae, Naoshi ^c   Arita, Kyohei ^d   Yoshimatsu, Masanori ^e   Iwai, Yukiko ^a   Fukui, Yoshinori ^a   Ueda, Koji ^b   Hamamoto, Ryuji ^e,f   Shirakawa, Masahiro ^e   Sasaki, Hiroyuki ^a   Nakamura, Yusuke ^e,f  

^a KYUSHU UNIVERSITY   (Japan)

^b INST OF PHYS AND CHEMICAL RESEARCH   (Japan)

^c RIKEN   (Japan)

^d KYOTO UNIVERSITY   (Japan)

^e THE UNIVERSITY OF TOKYO   (Japan)

^f University of Chicago   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL TRANSFERASE; AMINO ACID COMPOSITIONS; BINDING AFFINITIES; CHROMOSOMAL REARRANGEMENT; EPIGENETIC REGULATION; GENE TRANSCRIPTIONS; HISTONE H3; HISTONE MODIFICATION; HISTONE PROTEINS; HUMAN EMBRYONIC KIDNEY 293 CELLS; IN-VITRO; IN-VIVO; KNOCK OUTS; METHYLTRANSFERASES; MOUSE EMBRYOS; N-ACETYLATION; N-METHYLATION; OVER-EXPRESSION; SPLICING FACTORS;

ACETYLATION; ALKYLATION; AMINO ACIDS; BINDING ENERGY; HYDROXYLATION; TISSUE; TRANSCRIPTION;

PROTEINS;

5 HYDROXYLYSINE; ACYLTRANSFERASE; CARRIER PROTEINS AND BINDING PROTEINS; HISTONE; HISTONE H2A; HISTONE H2B; HISTONE H3; HISTONE H4; JUMONJI DOMAIN CONTAINING 6 PROTEIN; LYSINE; LYSYL 5; METHYLTRANSFERASE; UNCLASSIFIED DRUG;

ACETYLATION; AMINO ACID COMPOSITION; ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; CELL STRAIN HEK293; CONTROLLED STUDY; EMBRYO; HISTONE MODIFICATION; HYDROXYLATION; IN VITRO STUDY; KNOCKOUT MOUSE; METHYLATION; MOUSE; NONHUMAN; PLASMID; PRIORITY JOURNAL; PROTEIN EXPRESSION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; TESTIS; WILD TYPE;

ACETYLATION; ANIMALS; CHROMOSOMES, MAMMALIAN; HEK293 CELLS; HISTONES; HUMANS; HYDROXYLATION; JUMONJI DOMAIN-CONTAINING HISTONE DEMETHYLASES; LYSINE; MALE; METHYLATION; MICE; MICE, KNOCKOUT; ORGAN SPECIFICITY; PROTEIN PROCESSING, POST-TRANSLATIONAL; TESTIS; TRANSCRIPTION, GENETIC;

EID: 84874761632     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.433284     Document Type: Article

References (17)

1. Webby, C. J., Wolf, A., Gromak, N., Dreger, M., Kramer, H., Kessler, B., Nielsen, M. L., Schmitz, C., Butler, D. S., Yates, J. R., 3rd, Delahunty, C. M., Hahn, P., Lengeling, A., Mann, M., Proudfoot, N. J., Schofield, C. J., and Böttger, A. (2009) Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing. Science 325, 90-93
2. Hong, X., Zang, J., White, J., Wang, C., Pan, C. H., Zhao, R., Murphy, R. C., Dai, S., Henson, P., Kappler, J. W., Hagman, J., and Zhang, G. (2010) Interaction of JMJD6 with single-stranded RNA. Proc. Natl. Acad. Sci. U.S.A. 107, 14568-14572
3. Loenarz, C., and Schofield, C. J. (2008) Expanding chemical biology of 2-oxoglutarate oxygenases. Nat. Chem. Biol. 4, 152-156
4. Myllylä, R., Wang, C., Heikkinen, J., Juffer, A., Lampela, O., Risteli, M., Ruotsalainen, H., Salo, A., and Sipilä, L. (2007) Expanding the lysyl hydrox- ylase toolbox: new insights into the localization and activities of lysyl hydroxylase 3 (LH3). J. Cell. Physiol. 212, 323-329
5. Shi, Y., and Whetstine, J. R. (2007) Dynamic regulation of histone lysine methylation by demethylases. Mol. Cell 25, 1-14
6. Kunisaki, Y., Masuko, S., Noda, M., Inayoshi, A., Sanui, T., Harada, M., Sasazuki, T., and Fukui, Y. (2004) Defective fetal liver erythropoiesis and T lymphopoiesis in mice lacking the phosphatidylserine receptor. Blood 103, 3362-3364
7. Böse, J., Gruber, A. D., Helming, L., Schiebe, S., Wegener, I., Hafner, M., Beales, M., Köntgen, F., and Lengeling, A. (2004) The phosphatidylserine receptor has essential functions during embryogenesis but not in apoptotic cell removal. J. Biol. 3, 15
8. Unoki, M., Brunet, J., and Mousli, M. (2009) Drug discovery targeting epigenetic codes: the great potential of UHRF1, which links DNA methylation and histone modifications, as a drug target in cancers and toxoplasmosis. Biochem. Pharmacol. 78, 1279-1288
9. Masuda, A., and Dohmae, N. (2010) Automated Protein Hydrolysis Delivering Sample to a Solid Acid Catalyst for Amino Acid Analysis. Anal. Chem. 82, 8939-8945
10. Strahl, B. D., Ohba, R., Cook, R. G., and Allis, C. D. (1999) Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in Tetrahymena. Proc. Natl. Acad. Sci. U.S.A. 96, 14967-14972
11. Mantri, M., Loik, N. D., Hamed, R. B., Claridge, T. D., McCullagh, J. S., and Schofield, C. J. (2011) The 2-oxoglutarate-dependent oxygenase JMJD6 catalyses oxidation of lysine residues to give 5S-hydroxylysine residues. Chembiochem. 12, 531-534
12. Schiltz, R. L., Mizzen, C. A., Vassilev, A., Cook, R. G., Allis, C. D., and Nakatani, Y. (1999) Overlapping but distinct patterns of histone acetylation by the human coactivators p300 and PCAF within nucleosomal substrates. J. Biol. Chem. 274, 1189-1192
13. Hamamoto, R., Furukawa, Y., Morita, M., Iimura, Y., Silva, F. P., Li, M., Yagyu, R., and Nakamura, Y. (2004) SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells. Nat. Cell Biol. 6, 731-740
14. Han, G., Li, J., Wang, Y., Li, X., Mao, H., Liu, Y., and Chen, C. D. (2012) The hydroxylation activity of Jmjd6 is required for its homo-oligomerization. J. Cell. Biochem. 113, 1663-1670
15. Dillon, S. C., Zhang, X., Trievel, R. C., and Cheng, X. (2005) The SETdomain protein superfamily: protein lysine methyltransferases. Genome Biol. 6, 227
16. Zhang, X., Tamaru, H., Khan, S. I., Horton, J. R., Keefe, L. J., Selker, E. U., and Cheng, X. (2002) Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase. Cell 111, 117-127
17. Subramanian, K., Jia, D., Kapoor-Vazirani, P., Powell, D. R., Collins, R. E., Sharma, D., Peng, J., Cheng, X., and Vertino, P. M. (2008) Regulation of estrogen receptor by the SET7 lysine methyltransferase. Mol. Cell 30, 336-347