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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

DOT1L  -  DOT1-like histone H3K79 methyltransferase

Homo sapiens

Synonyms: DOT1, DOT1-like protein, H3-K79-HMTase, Histone H3-K79 methyltransferase, Histone-lysine N-methyltransferase, H3 lysine-79 specific, ...
 
 
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High impact information on DOT1L

  • We demonstrate that direct fusion of hDOT1L to MLL results in leukemic transformation in an hDOT1L methyltransferase activity-dependent manner [1].
  • hDOT1L links histone methylation to leukemogenesis [1].
  • The yeast Dot1 and its human counterpart, hDOT1L, methylate lysine 79 located within the globular domain of histone H3 [1].
  • Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase [2].
  • Additionally, we provide evidence that hDOT1L has an important role in the transformation process. hDOT1L contributes to CALM-AF10-mediated leukaemic transformation by preventing nuclear export of CALM-AF10 and by upregulating the Hoxa5 gene through H3K79 methylation [3].
 

Biological context of DOT1L

 

Associations of DOT1L with chemical compounds

 

Other interactions of DOT1L

  • Suppression of DOT1L, the enzyme that methylates Lys 79 of histone H3, also inhibited recruitment of 53BP1 to DSBs [4].
  • In this article, we will review the recent literature linking the key biochemical process of transcriptional elongation by RNA polymerase II to histone methylation by COMPASS, Dot1p, and Set2 methyltransferases [5].

References

  1. hDOT1L links histone methylation to leukemogenesis. Okada, Y., Feng, Q., Lin, Y., Jiang, Q., Li, Y., Coffield, V.M., Su, L., Xu, G., Zhang, Y. Cell (2005) [Pubmed]
  2. Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase. Min, J., Feng, Q., Li, Z., Zhang, Y., Xu, R.M. Cell (2003) [Pubmed]
  3. Leukaemic transformation by CALM-AF10 involves upregulation of Hoxa5 by hDOT1L. Okada, Y., Jiang, Q., Lemieux, M., Jeannotte, L., Su, L., Zhang, Y. Nat. Cell Biol. (2006) [Pubmed]
  4. Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks. Huyen, Y., Zgheib, O., Ditullio, R.A., Gorgoulis, V.G., Zacharatos, P., Petty, T.J., Sheston, E.A., Mellert, H.S., Stavridi, E.S., Halazonetis, T.D. Nature (2004) [Pubmed]
  5. Transcriptional elongation by RNA polymerase II and histone methylation. Gerber, M., Shilatifard, A. J. Biol. Chem. (2003) [Pubmed]
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