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Polycomb group multiprotein PRC2 complex; PRC2/EED-EZH2 complex; EZH2 histone methyltransferase complex (PcG)

Function: 1) distinct from PRC1 complex 2) maintenance of transcriptionally repressive state of genes throughout development 3) acts via chromatin remodeling & modification of histones, rendering chromatin heritably changed in its expressibility 4) able to mono-, di- & trimethylate Lys-27 of histone H3 5) minimum components required for methyltransferase activity of the PRC2/EED-EZH2 complex are EED, EZH2 & SUZ12 6) compacts chromatin in the absence of the methyltransferase cofactor S-adenosyl-L-methionine (SAM 7) the PRC2 complex may also interact with DNMT1, DNMT3A, DNMT3B & PHF1 via the EZH2 subunit & with SIRT1 via the SUZ12 subunit 8) may associate with HDAC1 9) recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems (putative) 10) genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1, CDKN2A & retinoic acid genes Structure: - subunits: EED, EZH2, RBBP4, RBBP7 & SUZ12 - EZH2 is the catalytic subunit Note: - two variants of the PRC2 complex have been described, termed PRC3 & PRC4 - each of the three complexes may include a different complement of EED isoforms, although the precise sequences of the isoforms in each complex have not been determined - the PRC2 & PRC4 complexes may also methylate Lys-26 of histone H1 in addition to Lys-27 of histone H3

Related

polycomb group protein (PcG)

General

histone N-methyltransferase molecular complex

Properties

COMPARTMENT: cell nucleus MOTIF: active site SUBUNITS: polycomb protein EED COMPARTMENT: cell nucleus MOTIF: EZH2 interaction {81-441} MOTIF: WD repeat {91-134} WD repeat {142-185} HIV1-MA interaction {149-303} WD repeat {188-228} WD repeat {234-275} HIV1-MA interaction {301-441} WD repeat {304-341} WD repeat {359-399} WD repeat {408-441} EZH2 polycomb protein SUZ12 COMPARTMENT: cell nucleus MOTIF: glycine-rich region {7-50} serine-rich region {51-59} MOTIF: serine residue (SEVERAL) alanine-rich region {60-67} MOTIF: alanine residue (SEVERAL) Zn finger C2H2-type SITE: 448-471 EFFECTOR-BOUND: Zn+2 Ser phosphorylation site {S546} VEFS-box. {563-639} histone-binding protein RBBP4 COMPARTMENT: cell nucleus MOTIF: acetylation site SITE: N-TERMINUS EFFECTOR-BOUND: acetyl WD repeat {122-155} WD repeat {175-206} WD repeat {225-256} WD repeat {271-302} WD repeat {315-346} WD repeat {372-403} histone-binding protein RBBP7 COMPARTMENT: cell nucleus MOTIF: WD repeat {121-152} WD repeat {174-205} WD repeat {224-255} WD repeat {270-301} WD repeat {314-345} Ser phosphorylation site {S354} WD repeat {371-402} Ser phosphorylation site {S413} Thr phosphorylation site {T416}

References

  1. UniProt :accession Q15022
  2. Kuzmichev A et al Different EZH2-containing complexes target methylation of histone H1 or nucleosomal histone H3. Mol Cell. 2004 Apr 23;14(2):183-93. PMID: 15099518
  3. Kuzmichev A et al Composition and histone substrates of polycomb repressive group complexes change during cellular differentiation. Proc Natl Acad Sci U S A. 2005 Feb 8;102(6):1859-64. PMID: 15684044
  4. Martin C et al Substrate preferences of the EZH2 histone methyltransferase complex. J Biol Chem. 2006 Mar 31;281(13):8365-70 PMID: 16431907

Components

histone-binding protein RBBP4; retinoblastoma-binding protein 4; RBBP-4; retinoblastoma-binding protein p48; chromatin assembly factor 1 subunit C; CAF-1 subunit C; chromatin assembly factor I p48 subunit; CAF-I 48 kD subunit; CAF-I p48; nucleosome-remodeling factor subunit RBAP48 (RBBP4, RbAp48) histone-binding protein RBBP7; retinoblastoma-binding protein 7; RBBP-7; retinoblastoma-binding protein p46; histone acetyltransferase type B subunit 2; nucleosome-remodeling factor subunit RBAP46 (RBBP7, RBAP46, HAT2) polycomb protein EED; hEED; WD protein associating with integrin cytoplasmic tails 1; WAIT-1 (EED) polycomb protein SUZ12 (suppressor of zeste 12 protein homolog, joined to JAZF1 protein, chromatin precipitated E2F target 9 protein, ChET 9 protein, SUZ12, CHET9, JJAZ1, KIAA0160)