3mts

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Chromo Domain of Human Histone-Lysine N-Methyltransferase SUV39H1

Structural highlights

3mts is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SUV91_HUMAN Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. Also weakly methylates histone H1 (in vitro). H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation.[1] [2] [3] [4] [5] [6]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

SUV39H1, the first identified histone lysine methyltransferase in human, is involved in chromatin modification and gene regulation. SUV39H1 contains a chromodomain in its N-terminus, which potentially plays a role in methyl-lysine recognition and SUV39H1 targeting. In this study, the structure of the chromodomain of human SUV39H1 was determined by X-ray crystallography. The SUV39H1 chromodomain displays a generally conserved structure fold compared with other solved chromodomains. However, different from other chromodomains, the SUV39H1 chromodomain possesses a much longer helix at its C-terminus. Furthermore, the SUV39H1 chromodomain was shown to recognize histone H3K9me2/3 specifically.

Crystal Structure of the Human SUV39H1 Chromodomain and Its Recognition of Histone H3K9me2/3.,Wang T, Xu C, Liu Y, Fan K, Li Z, Sun X, Ouyang H, Zhang X, Zhang J, Li Y, Mackenzie F, Min J, Tu X PLoS One. 2012;7(12):e52977. doi: 10.1371/journal.pone.0052977. Epub 2012 Dec 28. PMID:23285239[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
15 reviews cite this structure
Writing, erasing and reading histone lysine methylations.
Hyun et al. (2017)
14 more
19 other articles
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See Also

References

  1. ↑ Ait-Si-Ali S, Guasconi V, Fritsch L, Yahi H, Sekhri R, Naguibneva I, Robin P, Cabon F, Polesskaya A, Harel-Bellan A. A Suv39h-dependent mechanism for silencing S-phase genes in differentiating but not in cycling cells. EMBO J. 2004 Feb 11;23(3):605-15. Epub 2004 Feb 5. PMID:14765126 doi:http://dx.doi.org/10.1038/sj.emboj.7600074
  2. ↑ Carbone R, Botrugno OA, Ronzoni S, Insinga A, Di Croce L, Pelicci PG, Minucci S. Recruitment of the histone methyltransferase SUV39H1 and its role in the oncogenic properties of the leukemia-associated PML-retinoic acid receptor fusion protein. Mol Cell Biol. 2006 Feb;26(4):1288-96. PMID:16449642 doi:http://dx.doi.org/10.1128/MCB.26.4.1288-1296.2006
  3. ↑ Bradley SP, Kaminski DA, Peters AH, Jenuwein T, Stavnezer J. The histone methyltransferase Suv39h1 increases class switch recombination specifically to IgA. J Immunol. 2006 Jul 15;177(2):1179-88. PMID:16818776
  4. ↑ Mal AK. Histone methyltransferase Suv39h1 represses MyoD-stimulated myogenic differentiation. EMBO J. 2006 Jul 26;25(14):3323-34. Epub 2006 Jul 13. PMID:16858404 doi:http://dx.doi.org/10.1038/sj.emboj.7601229
  5. ↑ Vaquero A, Scher M, Erdjument-Bromage H, Tempst P, Serrano L, Reinberg D. SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation. Nature. 2007 Nov 15;450(7168):440-4. PMID:18004385 doi:http://dx.doi.org/10.1038/nature06268
  6. ↑ Murayama A, Ohmori K, Fujimura A, Minami H, Yasuzawa-Tanaka K, Kuroda T, Oie S, Daitoku H, Okuwaki M, Nagata K, Fukamizu A, Kimura K, Shimizu T, Yanagisawa J. Epigenetic control of rDNA loci in response to intracellular energy status. Cell. 2008 May 16;133(4):627-39. PMID:18485871 doi:S0092-8674(08)00459-5
  7. ↑ Wang T, Xu C, Liu Y, Fan K, Li Z, Sun X, Ouyang H, Zhang X, Zhang J, Li Y, Mackenzie F, Min J, Tu X. Crystal Structure of the Human SUV39H1 Chromodomain and Its Recognition of Histone H3K9me2/3. PLoS One. 2012;7(12):e52977. doi: 10.1371/journal.pone.0052977. Epub 2012 Dec 28. PMID:23285239 doi:10.1371/journal.pone.0052977

Contents


PDB ID 3mts

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