Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.11.27 extracted from

  • Polytarchou, C.; Pfau, R.; Hatziapostolou, M.; Tsichlis, P.
    The JmjC domain histone demethylase Ndy1 regulates redox homeostasis and protects cells from oxidative stress (2008), Mol. Cell. Biol., 28, 7451-7464 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.11.27

Cloned(Commentary)

Cloned (Comment) Organism
recombinant Ndy1 overexpression in mouse embryonic fibroblasts, quantitative real-time reverse transcriptase PCR expression analysis Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information Ndy1 knockdown by siRNA in fibroblasts. Significant reduction in K36-dimethylated histone H3 associated with the promoters of Nqo1 and Prdx4 genes in cells engineered to overexpress Ndy1 but not its CXXC deletion mutant. Trimethylation of histone H3 at K4 is also reduced in the promoter regions of both genes, though in a spatially restricted manner that spared the region near the transcription start site. But the effect of Ndy1 on histone H3K4 trimethylation is weak Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleus
-
 Mus musculus 5634
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[histone H3]-N6,N6-dimethyl-L-lysine 36 + 2-oxoglutarate + O2 Mus musculus
-
 [histone H3]-N6-methyl-L-lysine 36 + succinate + formaldehyde + CO2
-
 ?
[histone H3]-N6-methyl-L-lysine 36 + 2-oxoglutarate + O2 Mus musculus
-
 [histone H3]-L-lysine 36 + succinate + formaldehyde + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
fibroblast MEF Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is active on H3 trimethylated at K4 and dimethylated at K36, it might preferentially demethylate H3 trimethylated at K4 (EC 1.14.11.67) Mus musculus ?
-
 ?
[histone H3]-N6,N6-dimethyl-L-lysine 36 + 2-oxoglutarate + O2
-
 Mus musculus [histone H3]-N6-methyl-L-lysine 36 + succinate + formaldehyde + CO2
-
 ?
[histone H3]-N6-methyl-L-lysine 36 + 2-oxoglutarate + O2
-
 Mus musculus [histone H3]-L-lysine 36 + succinate + formaldehyde + CO2
-
 ?

Synonyms

Synonyms Comment Organism
JmjC domain histone demethylase
-
 Mus musculus
More see also EC 1.14.11.67 Mus musculus
Ndy1
-
 Mus musculus

General Information

General Information Comment Organism
malfunction Ndy1 knockdown by siRNA enhances sensitivity to oxidative stress, downregulation of Ndy1 activates the phosphorylation of AMPK, JNK, and p38MAPK and the cleavage of caspase-3 both before and after treatment with H2O2, Ndy1 overexpression protects cells against oxidative stress, overexpression of Ndy1 inhibits the phosphorylation of AMPK, JNK, and p38MAPK and the cleavage of caspase-3 both before and after treatment with H2O2. Knocking down Ndy1 sensitizes the cells to H2O2-induced oxidative stress. Genes Nqo1 and Prdx4 are direct Ndy1 targets. First, Ndy1 but not its DELTACXXC mutant binds specific regions in the promoters of both genes. Second, whereas Ndy1 upregulates their expression, the DELTACXXC mutant does not, suggesting that binding to the promoter region is necessary for their induction Mus musculus
metabolism Ndy1 epigenetically regulates several redox genes and the regulation of these genes by Ndy1 is responsible for the modulation of H2O2 levels and for the resistance of Ndy1-expressing cells to oxidative stress. Genes Nqo1 and Prdx4 are direct Ndy1 targets Mus musculus
physiological function the JmjC domain histone demethylase Ndy1 regulates redox homeostasis and protects cells from oxidative stress. 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 is sufficient to suppress the Ndy1 redox phenotype. The enzyme protects cells against oxidative stress by inhibiting reactive oxygen species-dependent signaling, overview. Ndy1 inhibits the oxidation of deoxyguanosine and DNA damage, and the accumulation of H2O2 in both H2O2-treated and untreated cells. Ndy1 enhances the antioxidant activity of cells. The gene Serpinb1b, upregulated by Ndy1, and gene IL-19, which is downregulated by Ndy1, play indirect roles in redox homeostasis, overview. Endogenous Ndy1 is a physiological redox regulator of the cellular response to oxidative stress. Ndy1 functions as an activator of transcription are in agreement with recently published data showing that Ndy1 promotes the transcriptional activation of the Hoxd1 gene. Ndy1 can also function as a repressor. Genes Nqo1 and Prdx4 are direct Ndy1 targets. First, Ndy1 but not its DELTACXXC mutant binds specific regions in the promoters of both genes. Second, whereas Ndy1 upregulates their expression, the DELTACXXC mutant does not, suggesting that binding to the promoter region is necessary for their induction Mus musculus