Regulation of MLL1 H3K4 methyltransferase activity by its core components

Nature Structural and Molecular Biology

Volumn 13, Issue 8, 2006, Pages 713-719

  Dou, Yali ^a   Milne, Thomas A ^a   Ruthenburg, Alexander J ^a,b   Lee, Seunghee ^d   Lee, Jae Woon ^d   Verdine, Gregory L ^b,c   Allis, C David ^a   Roeder, Robert G ^a  

^a ROCKEFELLER UNIVERSITY   (United States)

^b HARVARD UNIVERSITY   (United States)

^c HARVARD UNIVERSITY   (United States)

^d BAYLOR COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; HISTONE H3; HISTONE METHYLTRANSFERASE; LYSINE; MIXED LINEAGE LEUKEMIA PROTEIN; MIXED LINEAGE LEUKEMIA PROTEIN 1; PROTEIN; PROTEIN ASH2L; PROTEIN RBBP5; PROTEIN SET1; PROTEIN SUBUNIT; PROTEIN WDR5; TRYPTOPHAN; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL ANALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME REGULATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; ENZYME SUBUNIT; HUMAN; HUMAN CELL; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN METHYLATION; PROTEIN PROTEIN INTERACTION; TRANSCRIPTION INITIATION; TRANSCRIPTION REGULATION;

CATALYTIC DOMAIN; CELL LINE; DNA-BINDING PROTEINS; HETEROTRIMERIC GTP-BINDING PROTEINS; HISTONE-LYSINE N-METHYLTRANSFERASE; HISTONES; HUMANS; LYSINE; METHYLATION; MULTIPROTEIN COMPLEXES; MYELOID-LYMPHOID LEUKEMIA PROTEIN; NUCLEAR PROTEINS; RECOMBINANT PROTEINS; RNA INTERFERENCE; TRANSCRIPTION FACTORS;

MAMMALIA;

EID: 33746849256     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb1128     Document Type: Article

References (46)

1. Roguev, A. et al. The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4. EMBO J. 20, 7137-7148 (2001).
2. Briggs, S.D. et al. Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae. Genes Dev. 15, 3286-3295 (2001).
3. Zhang, K. et al. The Set1 methyltransferase opposes Ipl1 aurora kinase functions in chromosome segregation. Cell 122, 723-734 (2005).
4. Miller, T. et al. COMPASS: a complex of proteins associated with a trithorax-related SET domain protein. Proc. Natl. Acad. Sci. USA 98, 12902-12907 (2001).
5. Lee, J.H. & Skalnik, D.G. CpG-binding protein (CXXC finger protein 1) is a component of the mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue of the yeast Set1/COMPASS complex. J. Biol. Chem. 280, 41725-41731 (2005).
6. Nakamura, T. et al. ALL-1 is a histone methyltransferase that assembles a super-complex of proteins involved in transcriptional regulation. Mol. Cell 10, 1119-1128 (2002).
7. Dou, Y. et al. Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF. Cell 121, 873-885 (2005).
8. Hughes, C.M. et al. Menin associates with a trithorax family histone methyltransferase complex and with the hoxc8 locus. Mol. Cell 13, 587-597 (2004).
9. Goo, Y.H. et al. Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins. Mol. Cell. Biol. 23, 140-149 (2003).
10. Wysocka, J., Myers, M.P., Laherty, C.D., Eisenman, R.N. & Herr, W. Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1. Genes Dev. 17, 896-911 (2003).
11. Martin, C. & Zhang, Y. The diverse functions of histone lysine methylation. Nat. Rev. Mol. Cell Biol. 6, 838-849 (2005).
12. Yu, B.D., Hess, J.L., Horning, S.E., Brown, G.A. & Korsmeyer, S.J. Altered Hox expression and segmental identity in Mll-mutant mice. Nature 378, 505-508 (1995).
13. Glaser, S. et al. Multiple epigenetic maintenance factors implicated by the loss of Mll2 in mouse development. Development 133, 1423-1432 (2006).
14. Jenuwein, T., Laible, G., Dorn, R. & Reuter, G. SET domain proteins modulate chromatin domains in eu- and heterochromatin. Cell. Mol. Life Sci. 54, 80-93 (1998).
15. Flanagan, J.F. et al. Double chromodomains cooperate to recognize the methylated histone H3 tail. Nature 438, 1181-1185 (2005).
16. Wysocka, J. et al. A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling. Nature, advance online publication 21 May 2006 (doi:10.1038/nature04815).
17. Li, H. et al. Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF. Nature, advance online publication 21 May 2006 (doi:10.1038/nature04802).
18. Pena, P.V. et al. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Nature, advance online publication 21 May 2006 (doi:10.1038/nature04814).
19. Shi, X. et al. ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression. Nature, advance online publication 21 May 2006 (doi:10.1038/nature04835).
20. Ernst, P., Wang, J., Huang, M., Goodman, R.H. & Korsmeyer, S.J. MLL and CREB bind cooperatively to the nuclear coactivator CREB-binding protein. Mol. Cell. Biol. 21, 2249-2258 (2001).
21. Milne, T.A. et al. MLL associates specifically with a subset of transcriptionally active target genes. Proc. Natl. Acad. Sci. USA 102, 14765-14770 (2005).
22. Sun, Z.W. & Allis, C.D. Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature 418, 104-108 (2002).
23. Zhu, B. et al. Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation. Mol. Cell 20, 601-611 (2005).
24. Kim, J., Hake, S.B. & Roeder, R.G. The human homolog of yeast BRE1 functions as a transcriptional coactivator through direct activator interactions. Mol. Cell 20, 759-770 (2005).
25. Shahbazian, M.D., Zhang, K. & Grunstein, M. Histone H2B ubiquitylation controls processive methylation but not monomethylation by Dot1 and Set1. Mol. Cell 19, 271-277 (2005).
26. Sierra, J., Yoshida, T., Joazeiro, C.A. & Jones, K.A. The APC tumor suppressor counteracts beta-catenin activation and H3K4 methylation at Wnt target genes. Genes Dev. 20, 586-600 (2006).
27. Ng, H.H., Dole, S. & Struhl, K. The Rtf1 component of the Paf1 transcriptional elongation complex is required for ubiquitination of histone H2B. J. Biol. Chem. 278, 33625-33628 (2003).
28. Krogan, N.J. et al. The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation. Mol. Cell 11, 721-729 (2003).
29. Zhu, B. et al. The human PAF complex coordinates transcription with events downstream of RNA synthesis. Genes Dev. 19, 1668-1673 (2005).
30. Laribee, R.N. et al. BUR kinase selectively regulates H3 K4 trimethylation and H2B ubiquitylation through recruitment of the PAF elongation complex. Curr. Biol. 15, 1487-1493 (2005).
31. Morillon, A., Karabetsou, N., Nair, A. & Mellor, J. Dynamic lysine methylation on histone H3 defines the regulatory phase of gene transcription. Mol. Cell 18, 723-734 (2005).
32. Wysocka, J. et al. WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate development. Cell 121, 859-872 (2005).
33. Schneider, J. et al. Molecular regulation of histone H3 trimethylation by COMPASS and the regulation of gene expression. Mol. Cell 19, 849-856 (2005).
34. Ruthenburg, A.J. et al. Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex. Nat. Struct. Mol. Biol., advance online publication 9 July 2006 (doi:10.1038/nsmb1119).
35. Hamamoto, R. et al. SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells. Nat. Cell Biol. 6, 731-740 (2004).
36. Wang, H. et al. Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase. Mol. Cell 8, 1207-1217 (2001).
37. Hsieh, J.J., Ernst, P., Erdjument-Bromage, H., Tempst, P. & Korsmeyer, S.J. Proteolytic cleavage of MLL generates a complex of N- and C-terminal fragments that confers protein stability and subnuclear localization. Mol. Cell. Biol. 23, 186-194 (2003).
38. Yokoyama, A., Kitabayashi, I., Ayton, P.M., Cleary, M.L. & Ohki, M. Leukemia protooncoprotein MLL is proteolytically processed into 2 fragments with opposite transcriptional properties. Blood 100, 3710-3718 (2002).
39. Wang, H. et al. mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9 of histone H3 to cause transcriptional repression. Mol. Cell 12, 475-487 (2003).
40. Milne, T.A. et al. Menin and MLL cooperatively regulate expression of cyclin-dependent kinase inhibitors. Proc. Natl Acad. Sci. USA 102, 749-754 (2005).
41. Yokoyama, A. et al. The menin tumor suppressor protein is an essential oncogenic cofactor for MLL-associated leukemogenesis. Cell 123, 207-218 (2005).
42. Han, Z. et al. Structural basis for the specific recognition of methylated histone H3 lysine 4 by the WD-40 protein WDR5. Mol. Cell 22, 137-144 (2006).
43. Cao, R. et al. Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science 298, 1039-1043 (2002).
44. Muller, J. et al. Histone methyltransferase activity of a Drosophila Polycomb group repressor complex. Cell 111, 197-208 (2002).
45. Czermin, B. et al. Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites. Cell 111, 185-196 (2002).
46. Milne, T.A. et al. MLL targets SET domain methyltransferase activity to Hox gene promoters. Mol. Cell 10, 1107-1117 (2002).