Repository logo
 

Physical and functional interaction between SET1/COMPASS complex component CFP-1 and a Sin3S HDAC complex in C. elegans.

Published version
Peer-reviewed

Type

Article

Change log

Authors

Beurton, Flore 
Stempor, Przemyslaw  ORCID logo  https://orcid.org/0000-0002-9464-7475
Caron, Matthieu 
Appert, Alex 
Dong, Yan 

Abstract

The CFP1 CXXC zinc finger protein targets the SET1/COMPASS complex to non-methylated CpG rich promoters to implement tri-methylation of histone H3 Lys4 (H3K4me3). Although H3K4me3 is widely associated with gene expression, the effects of CFP1 loss vary, suggesting additional chromatin factors contribute to context dependent effects. Using a proteomics approach, we identified CFP1 associated proteins and an unexpected direct link between Caenorhabditis elegans CFP-1 and an Rpd3/Sin3 small (SIN3S) histone deacetylase complex. Supporting a functional connection, we find that mutants of COMPASS and SIN3 complex components genetically interact and have similar phenotypic defects including misregulation of common genes. CFP-1 directly binds SIN-3 through a region including the conserved PAH1 domain and recruits SIN-3 and the HDA-1/HDAC subunit to H3K4me3 enriched promoters. Our results reveal a novel role for CFP-1 in mediating interaction between SET1/COMPASS and a Sin3S HDAC complex at promoters.

Description

Keywords

Animals, Animals, Genetically Modified, Caenorhabditis elegans, Caenorhabditis elegans Proteins, DNA-Binding Proteins, Embryo, Nonmammalian, Histone-Lysine N-Methyltransferase, Multiprotein Complexes, Protein Binding, Sin3 Histone Deacetylase and Corepressor Complex, Trans-Activators

Journal Title

Nucleic Acids Res

Conference Name

Journal ISSN

0305-1048
1362-4962

Volume Title

47

Publisher

Oxford University Press (OUP)
Sponsorship
Wellcome Trust (101863/Z/13/Z)
Wellcome Trust (092096/Z/10/Z)
Cancer Research Uk (None)