GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

PMID:16055700

From GONUTS
Jump to: navigation, search
Citation

Ketel, CS, Andersen, EF, Vargas, ML, Suh, J, Strome, S and Simon, JA (2005) Subunit contributions to histone methyltransferase activities of fly and worm polycomb group complexes. Mol. Cell. Biol. 25:6857-68

Abstract

The ESC-E(Z) complex of Drosophila melanogaster Polycomb group (PcG) repressors is a histone H3 methyltransferase (HMTase). This complex silences fly Hox genes, and related HMTases control germ line development in worms, flowering in plants, and X inactivation in mammals. The fly complex contains a catalytic SET domain subunit, E(Z), plus three noncatalytic subunits, SU(Z)12, ESC, and NURF-55. The four-subunit complex is >1,000-fold more active than E(Z) alone. Here we show that ESC and SU(Z)12 play key roles in potentiating E(Z) HMTase activity. We also show that loss of ESC disrupts global methylation of histone H3-lysine 27 in fly embryos. Subunit mutations identify domains required for catalytic activity and/or binding to specific partners. We describe missense mutations in surface loops of ESC, in the CXC domain of E(Z), and in the conserved VEFS domain of SU(Z)12, which each disrupt HMTase activity but preserve complex assembly. Thus, the E(Z) SET domain requires multiple partner inputs to produce active HMTase. We also find that a recombinant worm complex containing the E(Z) homolog, MES-2, has robust HMTase activity, which depends upon both MES-6, an ESC homolog, and MES-3, a pioneer protein. Thus, although the fly and mammalian PcG complexes absolutely require SU(Z)12, the worm complex generates HMTase activity from a distinct partner set.

Links

PubMed PMC1190254 Online version:10.1128/MCB.25.16.6857-6868.2005

Keywords

Animals; Baculoviridae/metabolism; Blotting, Western; Caenorhabditis elegans; Catalytic Domain; Chromatin/chemistry; Chromosomal Proteins, Non-Histone/chemistry; DNA Methylation; DNA Mutational Analysis; Dose-Response Relationship, Drug; Drosophila Proteins/chemistry; Drosophila Proteins/physiology; Drosophila melanogaster; Histone-Lysine N-Methyltransferase/chemistry; Histone-Lysine N-Methyltransferase/metabolism; Histones/chemistry; Humans; Lysine/chemistry; Macromolecular Substances/chemistry; Methylation; Models, Biological; Molecular Chaperones/chemistry; Multiprotein Complexes/chemistry; Mutagenesis, Site-Directed; Mutation; Mutation, Missense; Protein Binding; Protein Methyltransferases; Protein Structure, Tertiary; Recombinant Fusion Proteins/chemistry; Recombinant Proteins/chemistry; Repressor Proteins; Retinoblastoma-Binding Protein 4; Zinc Fingers

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

DROME:EZ

enables

GO:0042054: histone methyltransferase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

DROME:EZ

enables

GO:0046976: histone methyltransferase activity (H3-K27 specific)

ECO:0000315: mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

DROME:EZ

part_of

GO:0035097: histone methyltransferase complex

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:EZ

involved_in

GO:0070734: histone H3-K27 methylation

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

DROME:ESC

part_of

GO:0035097: histone methyltransferase complex

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:ESC

involved_in

GO:0070734: histone H3-K27 methylation

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

DROME:CAF1

part_of

GO:0035097: histone methyltransferase complex

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:SUZ12

part_of

GO:0035097: histone methyltransferase complex

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete


See also

References

See Help:References for how to manage references in GONUTS.