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Arginine methylation of STAT1: A reassessment

Article Abstract:

A model is proposed stating that arginine 31 methylation of STAT1 enhances its DNA binding by reducing association with the specific inhibitor PIAS1, thus intensifying the growth-restraining activities of the interferons. The findings explain the interferon (IFN) insensitivity of cancer cells that accumulate high levels of the methyltransferase inhibitor methylthioadenosine (MTA).

Author: Vinkemeier, Uwe, Meissner, Torsten, Krause, Eberhard, Lodige, Inga
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2004
DNA-ligand interactions, DNA binding

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A crack in histone lysine methylation

Article Abstract:

Histone lysine methylation is considered to be a very stable modification with important uses in epigenetic gene control as well as for organizing chromatin domains. Studies show that the field of epigenetic control is ever changing as it is seen that histone lysine demethylase reverts an activating methyl mark to the unmodified state.

Author: Jenuwein, Thomas, Kubicek, Stefan
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2004
Lysine, Epigenetic inheritance

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hDOT1L links histone methylation to leukemogenesis

Article Abstract:

A study conducted demonstrates that the direct fusion of hDOT1L to mixed lineage leukemia (MLL) results in leukemic transformation in an hDOT1L methyltransferase activity-dependent manner. The results of the study suggest that the enzymatic activity of hDOT1L will provide a potential target for therapeutic intervention.

Author: Yi Zhang, Okada, Yuki, Qin Feng, Yihui Lin, Yaqiang Li, Qi Jiang, Coffield, Vernon M., Lishan Su, Guoliang Xu
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2005
Oncogenes

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Subjects list: Research, Methylation, Methyltransferases, Histones
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