2.50
Hdl Handle:
http://hdl.handle.net/10033/620687
Title:
Chromatin binding of Gcn5 in Drosophila is largely mediated by CP190.
Authors:
Ali, Tamer; Krüger, Marcus; Bhuju, Sabin; Jarek, Michael; Bartkuhn, Marek; Renkawitz, Rainer
Abstract:
Centrosomal 190 kDa protein (CP190) is a promoter binding factor, mediates long-range interactions in the context of enhancer-promoter contacts and in chromosomal domain formation. All Drosophila insulator proteins bind CP190 suggesting a crucial role in insulator function. CP190 has major effects on chromatin, such as depletion of nucleosomes, high nucleosomal turnover and prevention of heterochromatin expansion. Here, we searched for enzymes, which might be involved in CP190 mediated chromatin changes. Eighty percent of the genomic binding sites of the histone acetyltransferase Gcn5 are colocalizing with CP190 binding. Depletion of CP190 reduces Gcn5 binding to chromatin. Binding dependency was further supported by Gcn5 mediated co-precipitation of CP190. Gcn5 is known to activate transcription by histone acetylation. We used the dCas9 system to target CP190 or Gcn5 to a Polycomb repressed and H3K27me3 marked gene locus. Both, CP190 as well as Gcn5, activate this locus, thus supporting the model that CP190 recruits Gcn5 and thereby activates chromatin.
Affiliation:
Hel,holtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig, Germany.
Citation:
Chromatin binding of Gcn5 in Drosophila is largely mediated by CP190. 2016 Nucleic Acids Res.
Journal:
Nucleic acids research
Issue Date:
29-Nov-2016
URI:
http://hdl.handle.net/10033/620687
DOI:
10.1093/nar/gkw1178
PubMed ID:
27903907
Type:
Article
Language:
en
ISSN:
1362-4962
Appears in Collections:
publications of the research group genomeanalytics (GMAK)

Full metadata record

DC FieldValue Language
dc.contributor.authorAli, Tameren
dc.contributor.authorKrüger, Marcusen
dc.contributor.authorBhuju, Sabinen
dc.contributor.authorJarek, Michaelen
dc.contributor.authorBartkuhn, Mareken
dc.contributor.authorRenkawitz, Raineren
dc.date.accessioned2017-01-09T15:20:01Z-
dc.date.available2017-01-09T15:20:01Z-
dc.date.issued2016-11-29-
dc.identifier.citationChromatin binding of Gcn5 in Drosophila is largely mediated by CP190. 2016 Nucleic Acids Res.en
dc.identifier.issn1362-4962-
dc.identifier.pmid27903907-
dc.identifier.doi10.1093/nar/gkw1178-
dc.identifier.urihttp://hdl.handle.net/10033/620687-
dc.description.abstractCentrosomal 190 kDa protein (CP190) is a promoter binding factor, mediates long-range interactions in the context of enhancer-promoter contacts and in chromosomal domain formation. All Drosophila insulator proteins bind CP190 suggesting a crucial role in insulator function. CP190 has major effects on chromatin, such as depletion of nucleosomes, high nucleosomal turnover and prevention of heterochromatin expansion. Here, we searched for enzymes, which might be involved in CP190 mediated chromatin changes. Eighty percent of the genomic binding sites of the histone acetyltransferase Gcn5 are colocalizing with CP190 binding. Depletion of CP190 reduces Gcn5 binding to chromatin. Binding dependency was further supported by Gcn5 mediated co-precipitation of CP190. Gcn5 is known to activate transcription by histone acetylation. We used the dCas9 system to target CP190 or Gcn5 to a Polycomb repressed and H3K27me3 marked gene locus. Both, CP190 as well as Gcn5, activate this locus, thus supporting the model that CP190 recruits Gcn5 and thereby activates chromatin.en
dc.language.isoenen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.titleChromatin binding of Gcn5 in Drosophila is largely mediated by CP190.en
dc.typeArticleen
dc.contributor.departmentHel,holtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig, Germany.en
dc.identifier.journalNucleic acids researchen

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