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

BRENDA support

Literature summary for 2.1.1.356 extracted from

  • Stepanik, V.A.; Harte, P.J.
    A mutation in the E(Z) methyltransferase that increases trimethylation of histone H3 lysine 27 and causes inappropriate silencing of active Polycomb target genes (2012), Dev. Biol., 364, 249-258.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information the E(z)Trm mutation increases the histone H3 (K27) trimethylation efficiency of catalytic subunit E(Z) of Polycomb Repressive Complex 2 Drosophila melanogaster

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
embryo
-
Drosophila melanogaster
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + histone H3(K27) Drosophila Polycomb Repressive Complex 2 is a lysine methyltransferase that trimethylates histone H3 (K27) Drosophila melanogaster ?
-
?

Synonyms

Synonyms Comment Organism
Polycomb repressive complex 2
-
Drosophila melanogaster
PRC2
-
Drosophila melanogaster

General Information

General Information Comment Organism
malfunction mutations in the catalytic subunit E(Z) that abolish methyltransferase activity disrupt Polycomb silencing, causing derepression of Polycomb target genes in cells where they are normally silenced. Increased histone H3(K27) trimethylation activity of mutant E(Z)Trm causes the premature accumulation of trimethylated histone H3(K27) in early embryogenesis, predestining initially active Polycomb target genes to silencing once Polycomb silencing is initiated Drosophila melanogaster