scholarly journals Lung cancer-associated JmjC domain protein mdig suppresses formation of tri-methyl lysine 9 of histone H3

Cell Cycle ◽  
2009 ◽  
Vol 8 (13) ◽  
pp. 2101-2109 ◽  
Author(s):  
Yongju Lu ◽  
Kevin Beezhold ◽  
Qingshan Chang ◽  
Yadong Zhang ◽  
Yon Rojanasakul ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Histone H3 ◽  
Jmjc Domain ◽  
Domain Protein

scholarly journals Identification of Myc-associated protein with JmjC domain as a novel therapeutic target oncogene for lung cancer

2007 ◽  
Vol 6 (2) ◽  
pp. 542-551 ◽  
Author(s):  
Chie Suzuki ◽  
Koji Takahashi ◽  
Satoshi Hayama ◽  
Nobuhisa Ishikawa ◽  
Tatsuya Kato ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Therapeutic Target ◽  
Jmjc Domain ◽  
Novel Therapeutic

scholarly journals Jumonji C Domain Protein JMJ705-Mediated Removal of Histone H3 Lysine 27 Trimethylation Is Involved in Defense-Related Gene Activation in Rice

2013 ◽  
Vol 25 (11) ◽  
pp. 4725-4736 ◽  
Author(s):  
T. Li ◽  
X. Chen ◽  
X. Zhong ◽  
Y. Zhao ◽  
X. Liu ◽  
...  
Keyword(s):  
Gene Activation ◽  
Histone H3 ◽  
Related Gene ◽  
Defense Related Gene ◽  
Domain Protein

scholarly journals High expression of trimethylated histone H3 at lysine 27 predicts better prognosis in non-small cell lung cancer

2013 ◽  
Vol 43 (5) ◽  
pp. 1467-1480 ◽  
Author(s):  
XIAOHUI CHEN ◽  
NING SONG ◽  
KEITARO MATSUMOTO ◽  
ATSUSHI NANASHIMA ◽  
TAKESHI NAGAYASU ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Small Cell Lung Cancer ◽  
Cell Lung Cancer ◽  
Histone H3 ◽  
Small Cell ◽  
High Expression ◽  
Small Cell Lung

scholarly journals The JmjC Domain Histone Demethylase Ndy1 Regulates Redox Homeostasis and Protects Cells from Oxidative Stress

2008 ◽  
Vol 28 (24) ◽  
pp. 7451-7464 ◽  
Author(s):  
Christos Polytarchou ◽  
Raymond Pfau ◽  
Maria Hatziapostolou ◽  
Philip N. Tsichlis
Keyword(s):  
Redox Regulation ◽  
Replicative Senescence ◽  
Redox Homeostasis ◽  
Histone H3 ◽  
Quinone Oxidoreductase ◽  
Expression Of Genes ◽  
Genes Encoding ◽  
Jmjc Domain ◽  
Peptidase Inhibitor ◽  
Induced Apoptosis

ABSTRACT The histone H3 demethylase Ndy1/KDM2B protects cells from replicative senescence. Changes in the metabolism of reactive oxygen species (ROS) are important for establishing senescence, suggesting that Ndy1 may play a role in redox regulation. Here we show that Ndy1 protects from H2O2-induced apoptosis and G2/M arrest and inhibits ROS-mediated signaling and DNA damage, while knockdown of Ndy1 has the opposite effects. Consistent with these observations, whereas Ndy1 overexpression promotes H2O2 detoxification, Ndy1 knockdown inhibits it. Ndy1 promotes the expression of genes encoding the antioxidant enzymes aminoadipic semialdehyde synthase (Aass), NAD(P)H quinone oxidoreductase-1 (Nqo1), peroxiredoxin-4 (Prdx4), and serine peptidase inhibitor b1b (Serpinb1b) and represses the expression of interleukin-19. At least two of these genes (Nqo1 and Prdx4) are regulated directly by Ndy1, which binds to specific sites within their promoters and demethylates promoter-associated histone H3 dimethylated at K36 and histone H3 trimethylated at K4. Simultaneous knockdown of Aass, Nqo1, Prdx4, and Serpinb1b in Ndy1-expressing cells to levels equivalent to those detected in control cells was sufficient to suppress the Ndy1 redox phenotype.

scholarly journals A novel SWIM domain protein ZSWIM5 inhibits the malignant progression of non-small-cell lung cancer

2018 ◽  
Vol Volume 10 ◽  
pp. 3245-3254 ◽  
Author(s):  
Ke Xu ◽  
Bin Liu ◽  
Yegang Ma ◽  
Baojin Xu ◽  
Xiaojing Xing
Keyword(s):  
Lung Cancer ◽  
Small Cell Lung Cancer ◽  
Cell Lung Cancer ◽  
Small Cell ◽  
Malignant Progression ◽  
Small Cell Lung ◽  
Domain Protein

scholarly journals JMJ14, a JmjC domain protein, is required for RNA silencing and cell-to-cell movement of an RNA silencing signal in Arabidopsis

2010 ◽  
Vol 24 (10) ◽  
pp. 986-991 ◽  
Author(s):  
I. R. Searle ◽  
O. Pontes ◽  
C. W. Melnyk ◽  
L. M. Smith ◽  
D. C. Baulcombe
Keyword(s):  
Rna Silencing ◽  
Cell Movement ◽  
Jmjc Domain ◽  
Domain Protein

scholarly journals PHF8 Targets Histone Methylation and RNA Polymerase II To Activate Transcription

2010 ◽  
Vol 30 (13) ◽  
pp. 3286-3298 ◽  
Author(s):  
Klaus Fortschegger ◽  
Petra de Graaf ◽  
Nikolay S. Outchkourov ◽  
Frederik M. A. van Schaik ◽  
H. T. Marc Timmers ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Cleft Lip ◽  
High Throughput Sequencing ◽  
Histone H3 ◽  
Direct Interaction ◽  
Activation Function ◽  
Transcription Start Sites ◽  
Jmjc Domain ◽  
Recognition Motifs

ABSTRACT Mutations in PHF8 are associated with X-linked mental retardation and cleft lip/cleft palate. PHF8 contains a plant homeodomain (PHD) in its N terminus and is a member of a family of JmjC domain-containing proteins. While PHDs can act as methyl lysine recognition motifs, JmjC domains can catalyze lysine demethylation. Here, we show that PHF8 is a histone demethylase that removes repressive histone H3 dimethyl lysine 9 marks. Our biochemical analysis revealed specific association of the PHF8 PHD with histone H3 trimethylated at lysine 4 (H3K4me3). Chromatin immunoprecipitation followed by high-throughput sequencing indicated that PHF8 is enriched at the transcription start sites of many active or poised genes, mirroring the presence of RNA polymerase II (RNAPII) and of H3K4me3-bearing nucleosomes. We show that PHF8 can act as a transcriptional coactivator and that its activation function largely depends on binding of the PHD to H3K4me3. Furthermore, we present evidence for direct interaction of PHF8 with the C-terminal domain of RNAPII. Importantly, a PHF8 disease mutant was defective in demethylation and in coactivation. This is the first demonstration of a chromatin-modifying enzyme that is globally recruited to promoters through its association with H3K4me3 and RNAPII.

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