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  • 1
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    Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27 in histone H3 (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-10-15
    Description: Enhancer of Zeste homolog 2 (EZH2) is a methyltransferase that plays an important role in many biological processes through its ability to trimethylate lysine 27 in histone H3. Here, we show that Akt phosphorylates EZH2 at serine 21 and suppresses its methyltransferase activity by impeding EZH2 binding to histone H3, which results in a decrease of lysine 27 trimethylation and derepression of silenced genes. Our results imply that Akt regulates the methylation activity, through phosphorylation of EZH2, which may contribute to oncogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cha, Tai-Lung -- Zhou, Binhua P -- Xia, Weiya -- Wu, Yadi -- Yang, Cheng-Chieh -- Chen, Chun-Te -- Ping, Bo -- Otte, Arie P -- Hung, Mien-Chie -- P01 099031/PHS HHS/ -- R01 109311/PHS HHS/ -- New York, N.Y. -- Science. 2005 Oct 14;310(5746):306-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Oncology, the University of Texas M. D. Anderson Cancer Center, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16224021" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; COS Cells ; Cell Line ; Cell Transformation, Neoplastic ; Cercopithecus aethiops ; Chromones/pharmacology ; DNA-Binding Proteins ; Enzyme Inhibitors/pharmacology ; Gene Expression Regulation ; HeLa Cells ; Histone-Lysine N-Methyltransferase/metabolism ; Histones/*metabolism ; Homeodomain Proteins/genetics ; Humans ; Lysine/*metabolism ; Methylation ; Mice ; Molecular Sequence Data ; Morpholines/pharmacology ; Phosphorylation ; Polycomb Repressive Complex 2 ; Protein Binding ; Protein Methyltransferases ; Protein-Serine-Threonine Kinases/antagonists & inhibitors/*metabolism ; Proteins/*metabolism ; Proto-Oncogene Proteins/antagonists & inhibitors/*metabolism ; Proto-Oncogene Proteins c-akt ; Serine/metabolism ; Transcription Factors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    A 5-methylcytosine DNA glycosylase/lyase demethylates the retrotransposon Tos17 and promotes its transposition in rice [Plant Biology] (2011)
    National Academy of Sciences
    Details
    Publication Date: 2011-09-14
    Description: DNA 5-methylcytosine (5-meC) is an important epigenetic mark for transcriptional gene silencing in many eukaryotes. In Arabidopsis, 5-meC DNA glycosylase/lyases actively remove 5-meC to counteract transcriptional gene silencing in a locus-specific manner, and have been suggested to maintain the expression of transposons. However, it is unclear whether plant DNA demethylases can promote the transposition of transposons. Here we report the functional characterization of the DNA glycosylase/lyase DNG701 in rice. DNG701 encodes a large (1,812 amino acid residues) DNA glycosylase domain protein. Recombinant DNG701 protein showed 5-meC DNA glycosylase and lyase activities in vitro. Knockout or knockdown of DNG701 in rice plants led to DNA hypermethylation and reduced expression of the retrotransposon Tos17. Tos17 showed less transposition in calli derived from dng701 knockout mutant seeds compared with that in wild-type calli. Overexpression of DNG701 in both rice calli and transgenic plants substantially reduced DNA methylation levels of Tos17 and enhanced its expression. The overexpression also led to more frequent transposition of Tos17 in calli. Our results demonstrate that rice DNG701 is a 5-meC DNA glycosylase/lyase responsible for the demethylation of Tos17 and this DNA demethylase plays a critical role in promoting Tos17 transposition in rice calli.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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