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Gene Review

SUV39H1  -  suppressor of variegation 3-9 homolog 1...

Homo sapiens

Synonyms: H3-K9-HMTase 1, Histone H3-K9 methyltransferase 1, Histone-lysine N-methyltransferase SUV39H1, KMT1A, Lysine N-methyltransferase 1A, ...
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Disease relevance of SUV39H1

  • We found that RD2 contacts SUV39H1, a histone methyltransferase, via two motifs and that endogenous Suv39h1 associates with a Runx1-regulated repression element in murine erythroleukemia cells [1].

High impact information on SUV39H1


Biological context of SUV39H1

  • The 13-mer peptide containing a consensus sequence for binding to the dimer surface formed by the chromo shadow domains inhibited interaction between mHP1 alpha and SUV39H1 [6].
  • In addition, we show that SUV39H1 is phosphorylated specifically at the G(1)/S cell cycle transition and when forcibly expressed suppresses cell growth [7].
  • A possible role in chromatin-mediated gene silencing is supported by the localization of exogenously expressed SUV39H1 to nuclear bodies with morphologic features suggestive of heterochromatin in interphase cells [7].
  • SUV39H1, a mammalian ortholog of Drosophila Su(var)3-9, contains both SET and chromo domains, signature motifs for proteins that contribute to epigenetic control of gene expression through effects on the regional organization of chromatin structure [7].
  • In addition, SUV39H1 selectively associates with the active centromere of a dicentric chromosome and also with a neocentromere [8].

Anatomical context of SUV39H1

  • Together, these data provide evidence for a role of the SUV39H1 HMTase during the mammalian development and indicate a possible function for higher-order chromatin in contributing to the balance between proliferation and differentiation potentials of progenitor cells [9].

Associations of SUV39H1 with chemical compounds

  • This effect is mediated by the previously described association of PML-RAR with chromatin-modifying enzymes (histone deacetylases and DNA methyltransferases) and by recruitment of the histone methyltransferase SUV39H1, responsible for trimethylation of lysine 9 of histone H3 [10].
  • A yeast two-hybrid and a glutathione S-transferase pull-down study indicated that the chromo shadow domain of mHP1 alpha directly interacts with the N-terminal 39 amino acid stretch of SUV39H1 [6].
  • Here, we found that LANA interacts with SUV39H1 histone methyltransferase, a key component of heterochromatin formation, as determined by use of a DNA pull-down assay with a biotinylated DNA fragment that contained a LANA-specific binding sequence and a maltose-binding protein pull-down assay [11].
  • Similarly, the methylated peptide was a competitive inhibitor of the unmethylated peptide and a mixed inhibitor of AdoMet, suggesting a random mechanism in a bi-bi reaction for recombinant SUV39H1 in which either substrate can bind to the enzyme first and either product can release first [12].
  • Product inhibition studies with SUV39H1 showed that S-adenosyl-l-homocysteine is a competitive inhibitor of S-adenosyl-l-methionine and a mixed inhibitor of substrate peptide [12].

Physical interactions of SUV39H1

  • We find that SUV39H1 also binds to Dnmt1 and, consistent with these interactions, SUV39H1 can purify DNA methyltransferase activity from nuclear extracts [13].

Enzymatic interactions of SUV39H1

  • Growth suppression as well as the ability of SUV39H1 to form nuclear bodies and silence transcription are antagonized by the oncogenic antiphosphatase Sbf1 that when hyperexpressed interacts with the SET domain and stabilizes the phosphorylated form of SUV39H1 [7].

Other interactions of SUV39H1


Analytical, diagnostic and therapeutic context of SUV39H1

  • Although co-localization of HP1 and SUV39H1 has been evident in immunostaining and immunoprecipitation experiments, direct protein-protein interactions have remained to be characterized [6].
  • RESULTS: Sequence analysis of the break points showed that the translocation was fully balanced and only one gene on chromosome 9 was disrupted--Euchromatin Histone Methyl Transferase1 (Eu-HMTase1)--encoding a histone H3 lysine 9 methyltransferase (H3-K9 HMTase) [15].


  1. RUNX1 associates with histone deacetylases and SUV39H1 to repress transcription. Reed-Inderbitzin, E., Moreno-Miralles, I., Vanden-Eynden, S.K., Xie, J., Lutterbach, B., Durst-Goodwin, K.L., Luce, K.S., Irvin, B.J., Cleary, M.L., Brandt, S.J., Hiebert, S.W. Oncogene (2006) [Pubmed]
  2. Rb targets histone H3 methylation and HP1 to promoters. Nielsen, S.J., Schneider, R., Bauer, U.M., Bannister, A.J., Morrison, A., O'Carroll, D., Firestein, R., Cleary, M., Jenuwein, T., Herrera, R.E., Kouzarides, T. Nature (2001) [Pubmed]
  3. Regulation of chromatin structure by site-specific histone H3 methyltransferases. Rea, S., Eisenhaber, F., O'Carroll, D., Strahl, B.D., Sun, Z.W., Schmid, M., Opravil, S., Mechtler, K., Ponting, C.P., Allis, C.D., Jenuwein, T. Nature (2000) [Pubmed]
  4. Direct interaction between DNMT1 and G9a coordinates DNA and histone methylation during replication. Est??ve, P.O., Chin, H.G., Smallwood, A., Feehery, G.R., Gangisetty, O., Karpf, A.R., Carey, M.F., Pradhan, S. Genes Dev. (2006) [Pubmed]
  5. Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase. Wang, H., Cao, R., Xia, L., Erdjument-Bromage, H., Borchers, C., Tempst, P., Zhang, Y. Mol. Cell (2001) [Pubmed]
  6. Self-interaction of heterochromatin protein 1 is required for direct binding to histone methyltransferase, SUV39H1. Yamamoto, K., Sonoda, M. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  7. Set domain-dependent regulation of transcriptional silencing and growth control by SUV39H1, a mammalian ortholog of Drosophila Su(var)3-9. Firestein, R., Cui, X., Huie, P., Cleary, M.L. Mol. Cell. Biol. (2000) [Pubmed]
  8. Mitotic phosphorylation of SUV39H1, a novel component of active centromeres, coincides with transient accumulation at mammalian centromeres. Aagaard, L., Schmid, M., Warburton, P., Jenuwein, T. J. Cell. Sci. (2000) [Pubmed]
  9. Over-expression of the SUV39H1 histone methyltransferase induces altered proliferation and differentiation in transgenic mice. Czvitkovich, S., Sauer, S., Peters, A.H., Deiner, E., Wolf, A., Laible, G., Opravil, S., Beug, H., Jenuwein, T. Mech. Dev. (2001) [Pubmed]
  10. Recruitment of the histone methyltransferase SUV39H1 and its role in the oncogenic properties of the leukemia-associated PML-retinoic acid receptor fusion protein. Carbone, R., Botrugno, O.A., Ronzoni, S., Insinga, A., Di Croce, L., Pelicci, P.G., Minucci, S. Mol. Cell. Biol. (2006) [Pubmed]
  11. Accumulation of heterochromatin components on the terminal repeat sequence of Kaposi's sarcoma-associated herpesvirus mediated by the latency-associated nuclear antigen. Sakakibara, S., Ueda, K., Nishimura, K., Do, E., Ohsaki, E., Okuno, T., Yamanishi, K. J. Virol. (2004) [Pubmed]
  12. Catalytic properties and kinetic mechanism of human recombinant Lys-9 histone H3 methyltransferase SUV39H1: participation of the chromodomain in enzymatic catalysis. Chin, H.G., Patnaik, D., Estève, P.O., Jacobsen, S.E., Pradhan, S. Biochemistry (2006) [Pubmed]
  13. The DNA methyltransferases associate with HP1 and the SUV39H1 histone methyltransferase. Fuks, F., Hurd, P.J., Deplus, R., Kouzarides, T. Nucleic Acids Res. (2003) [Pubmed]
  14. Activation of the beta globin locus by transcription factors and chromatin modifiers. McMorrow, T., van den Wijngaard, A., Wollenschlaeger, A., van de Corput, M., Monkhorst, K., Trimborn, T., Fraser, P., van Lohuizen, M., Jenuwein, T., Djabali, M., Philipsen, S., Grosveld, F., Milot, E. EMBO J. (2000) [Pubmed]
  15. Disruption of the gene Euchromatin Histone Methyl Transferase1 (Eu-HMTase1) is associated with the 9q34 subtelomeric deletion syndrome. Kleefstra, T., Smidt, M., Banning, M.J., Oudakker, A.R., Van Esch, H., de Brouwer, A.P., Nillesen, W., Sistermans, E.A., Hamel, B.C., de Bruijn, D., Fryns, J.P., Yntema, H.G., Brunner, H.G., de Vries, B.B., van Bokhoven, H. J. Med. Genet. (2005) [Pubmed]
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