<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Beurton F</submitter><funding>Wellcome Trust Senior Research Fellowship</funding><funding>Proteomics French Infrastructure</funding><funding>Fondation ARC</funding><funding>Cancer Research UK</funding><funding>Agence Nationale de la Recherche</funding><funding>Labex GRAL</funding><funding>Wellcome Trust</funding><pagination>11164-11180</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6868398</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>47(21)</volume><pubmed_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 dom</pubmed_abstract><journal>Nucleic acids research</journal><pubmed_title>Physical and functional interaction between SET1/COMPASS complex component CFP-1 and a Sin3S HDAC complex in C. elegans.</pubmed_title><pmcid>PMC6868398</pmcid><funding_grant_id>15-CE12-0018-01</funding_grant_id><funding_grant_id>155265</funding_grant_id><funding_grant_id>ANR-10-LABX-49-01</funding_grant_id><funding_grant_id>101863/Z/13/Z</funding_grant_id><funding_grant_id>C6946/A14492</funding_grant_id><funding_grant_id>092096</funding_grant_id><funding_grant_id>101863</funding_grant_id><pubmed_authors>Coute Y</pubmed_authors><pubmed_authors>Caron M</pubmed_authors><pubmed_authors>Spichty M</pubmed_authors><pubmed_authors>Dong Y</pubmed_authors><pubmed_authors>Huang N</pubmed_authors><pubmed_authors>Beurton F</pubmed_authors><pubmed_authors>Appert A</pubmed_authors><pubmed_authors>Cluet D</pubmed_authors><pubmed_authors>Stempor P</pubmed_authors><pubmed_authors>Bedet C</pubmed_authors><pubmed_authors>Polveche H</pubmed_authors><pubmed_authors>Herbette M</pubmed_authors><pubmed_authors>Ahringer J</pubmed_authors><pubmed_authors>Palladino F</pubmed_authors><pubmed_authors>Chen RA</pubmed_authors></additional><is_claimable>false</is_claimable><name>Physical and functional interaction between SET1/COMPASS complex component CFP-1 and a Sin3S HDAC complex in C. elegans.</name><description>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 dom</description><dates><release>2019-01-01T00:00:00Z</release><publication>2019 Dec</publication><modification>2026-04-07T19:17:58.437Z</modification><creation>2020-05-21T20:11:55Z</creation></dates><accession>S-EPMC6868398</accession><cross_references><pubmed>31602465</pubmed><doi>10.1093/nar/gkz880</doi></cross_references></HashMap>