EC 2.1.1.356 - [histone H3]-lysine27 N-trimethyltransferase

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IntEnz Enzyme Nomenclature
EC 2.1.1.356

Names

Accepted name:
[histone H3]-lysine27 N-trimethyltransferase
Systematic name:
S-adenosyl-L-methionine:[histone H3]-L-lysine27 N6-methyltransferase

Reaction

Comments:

This entry describes enzymes that successively methylate the L-lysine27 residue of histone H3 (H3K27), ultimately generating a trimethylated form. These modifications influence the binding of chromatin-associated proteins. The methylation of lysine27 leads to transcriptional repression of the affected target genes. The enzyme associates with other proteins to form a complex that is essential for activity. The enzyme can also methylate some non-histone proteins. Formerly EC 2.1.1.43.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB

References

  1. Cao, R., Wang, L., Wang, H., Xia, L., Erdjument-Bromage, H., Tempst, P., Jones, R. S., Zhang, Y.
    Role of histone H3 lysine 27 methylation in Polycomb-group silencing.
    Science 298: 1039-1043 (2002). [PMID: 12351676]
  2. Kuzmichev, A., Nishioka, K., Erdjument-Bromage, H., Tempst, P., Reinberg, D.
    Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein.
    Genes Dev. 16: 2893-2905 (2002). [PMID: 12435631]
  3. Kirmizis, A., Bartley, S. M., Kuzmichev, A., Margueron, R., Reinberg, D., Green, R., Farnham, P. J.
    Silencing of human polycomb target genes is associated with methylation of histone H3 Lys 27.
    Genes Dev. 18: 1592-1605 (2004). [PMID: 15231737]
  4. Schlesinger, Y., Straussman, R., Keshet, I., Farkash, S., Hecht, M., Zimmerman, J., Eden, E., Yakhini, Z., Ben-Shushan, E., Reubinoff, B. E., Bergman, Y., Simon, I., Cedar, H.
    Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for de novo methylation in cancer.
    Nat. Genet. 39: 232-236 (2007). [PMID: 17200670]
  5. Shen, X., Liu, Y., Hsu, Y. J., Fujiwara, Y., Kim, J., Mao, X., Yuan, G. C., Orkin, S. H.
    EZH1 mediates methylation on histone H3 lysine 27 and complements EZH2 in maintaining stem cell identity and executing pluripotency.
    Mol. Cell 32: 491-502 (2008). [PMID: 19026780]
  6. Ezhkova, E., Lien, W. H., Stokes, N., Pasolli, H. A., Silva, J. M., Fuchs, E.
    EZH1 and EZH2 cogovern histone H3K27 trimethylation and are essential for hair follicle homeostasis and wound repair.
    Genes Dev. 25: 485-498 (2011). [PMID: 21317239]

[EC 2.1.1.356 created 1976 as EC 2.1.1.43, modified 1982, modified 1983, part transferred 2019 to EC 2.1.1.356]