Protein arginine methyltransferase 7 has a novel homodimer-like structure formed by tandem repeats

FEBS Letters

Volumn 588, Issue 10, 2014, Pages 1942-1948

  Hasegawa, Morio ^a   Toma Fukai, Sachiko ^a   Kim, Jun Dal ^b   Fukamizu, Akiyoshi ^b   Shimizu, Toshiyuki ^a,c  

^a UNIVERSITY OF TOKYO   (Japan)

^b UNIVERSITY OF TSUKUBA   (Japan)

^c JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

Protein arginine methyltransferase; S adenosyl l homocysteine; X ray crystallography

Indexed keywords

ADENOSYLHOMOCYSTEINASE; PROTEIN ARGININE METHYLTRANSFERASE; PROTEIN ARGININE METHYLTRANSFERASE 7; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CAENORHABDITIS ELEGANS; CARBOXY TERMINAL SEQUENCE; COLUMN CHROMATOGRAPHY; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; GEL FILTRATION CHROMATOGRAPHY; MUTAGENESIS; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STRUCTURE; TANDEM REPEAT; X RAY CRYSTALLOGRAPHY;

CAENORHABDITIS ELEGANS;

PROTEIN ARGININE METHYLTRANSFERASE; S-ADENOSYL-L-HOMOCYSTEINE; X-RAY CRYSTALLOGRAPHY;

ANIMALS; ARGININE; BINDING SITES; CAENORHABDITIS ELEGANS; CAENORHABDITIS ELEGANS PROTEINS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; MUTATION; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN-ARGININE N-METHYLTRANSFERASES; SCATTERING, SMALL ANGLE; TANDEM REPEAT SEQUENCES;

EID: 84900408448     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2014.03.053     Document Type: Article

References (25)

1. M.T. Bedford, and S.G. Clarke Protein arginine methylation in mammals: who, what, and why Mol. Cell 33 2009 1 13
2. C.I. Zurita-Lopez, T. Sandberg, R. Kelly, and S.G. Clarke Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming omega-NG-monomethylated arginine residues J. Biol. Chem. 287 2012 7859 7870
3. Y. Feng et al. Mammalian protein arginine methyltransferase 7 (PRMT7) specifically targets RXR Sites in lysine- and arginine-rich regions J. Biol. Chem. 288 2013 37010 37025
4. Y. Yang, and M.T. Bedford Protein arginine methyltransferases and cancer Nat. Rev. Cancer. 13 2013 37 50
5. Y. Auclair, and S. Richard The role of arginine methylation in the DNA damage response DNA repair 12 2013 459 465
6. G.B. Gonsalvez, L. Tian, J.K. Ospina, F.M. Boisvert, A.I. Lamond, and A.G. Matera Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins J. Cell. Biol. 178 2007 733 740
7. V. Karkhanis, L. Wang, S. Tae, Y.J. Hu, A.N. Imbalzano, and S. Sif Protein arginine methyltransferase 7 regulates cellular response to DNA damage by methylating promoter histones H2A and H4 of the polymerase delta catalytic subunit gene, POLD1 J. Biol. Chem. 287 2012 29801 29814
8. N. Buhr, C. Carapito, C. Schaeffer, E. Kieffer, A. Van Dorsselaer, and S. Viville Nuclear proteome analysis of undifferentiated mouse embryonic stem and germ cells Electrophoresis 29 2008 2381 2390
9. S.S. Dhar, S.H. Lee, P.Y. Kan, P. Voigt, L. Ma, X. Shi, D. Reinberg, and M.G. Lee Trans-tail regulation of MLL4-catalyzed H3K4 methylation by H4R3 symmetric dimethylation is mediated by a tandem PHD of MLL4 Genes Dev. 26 2012 2749 2762
10. M. Thomassen, Q. Tan, and T.A. Kruse Gene expression meta-analysis identifies chromosomal regions and candidate genes involved in breast cancer metastasis Breast cancer Res. Treat. 113 2009 239 249
11. X. Zhang, and X. Cheng Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides Structure 11 2003 509 520
12. T.B. Miranda, M. Miranda, A. Frankel, and S. Clarke PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity J. Biol. Chem. 279 2004 22902 22907
13. Y. Takahashi, H. Daitoku, A. Yokoyama, K. Nakayama, J.D. Kim, and A. Fukamizu The C. elegans PRMT-3 possesses a type III protein arginine methyltransferase activity J. Recept. Signal Transduct. Res. 31 2011 168 172
14. Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
15. C. Vonrhein, E. Blanc, P. Roversi, and G. Bricogne Automated structure solution with autoSHARP Methods Mol. Biol. 364 2007 215 230
16. A.J. McCoy, R.W. Grosse-Kunstleve, P.D. Adams, M.D. Winn, L.C. Storoni, and R.J. Read Phaser crystallographic software J. Appl. Crystallogr. 40 2007 658 674
17. G. Langer, S.X. Cohen, V.S. Lamzin, and A. Perrakis Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7 Nat. Protoc. 3 2008 1171 1179
18. P. Emsley, and K. Cowtan Coot: model-building tools for molecular graphics Acta Crystallogr. D Biol. Crystallogr. 60 2004 2126 2132
19. G.N. Murshudov, A.A. Vagin, and E.J. Dodson Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallogr. D Biol. Crystallogr. 53 1997 240 255
20. R.A. Laskowski, M.W. MacArthur, D.S. Moss, and J.M. Thornton PROCHECK: a program to check the stereochemical quality of protein struc-tures J. Appl. Crystallogr. 26 1993 283 291
21. P.V. Konarev, V.V. Volkov, A.V. Sokolova, M.H.J. Koch, and D.I. Svergun PRIMUS: a Windows PC-based system for small-angle scattering data analysis J. Appl. Crystallogr. 36 2003 1277 1282
22. X. Zhang, L. Zhou, and X. Cheng Crystal structure of the conserved core of protein arginine methyltransferase PRMT3 EMBO J. 19 2000 3509 3519
23. L. Sun, M. Wang, Z. Lv, N. Yang, Y. Liu, S. Bao, W. Gong, and R.M. Xu Structural insights into protein arginine symmetric dimethylation by PRMT5 Proc. Natl. Acad. Sci. U.S.A. 108 2011 20538 20543
24. S. Antonysamy et al. Crystal structure of the human PRMT5:MEP50 complex Proc. Natl. Acad. Sci. U.S.A. 109 2012 17960 17965
25. A. Frankel, N. Yadav, J. Lee, T.L. Branscombe, S. Clarke, and M.T. Bedford The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity J. Biol. Chem. 277 2002 3537 3543