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Ass. Lect. Tamer Ali :: Publications:

Chromatin Binding of Gcn5 in Drosophila is Largely Mediated by CP190
Authors: Ali, Tamer; Krüger, Marcus; Bhuju, Sabin; Jarek, Michael; Bartkuhn, Marek; Renkawitz, Rainer
Year: 2016
Keywords: CP190, Gcn5, dCas9, RNA-Seq, ChIP-Seq
Journal: Nucleic Acid Research
Volume: in press
Issue: Not Available
Pages: Not Available
Publisher: Not Available
Local/International: International
Paper Link: Not Available
Full paper Tamer Ali_Nucl. Acids Res.-2016-Ali-nar_gkw1178.pdf
Supplementary materials Not Available

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. 80% of the genomic binding sites of the histone acetyltransferase Gcn5 are colocalizing with CP190 binding. Depletion of CP190 reduces the number of Gcn5 binding sites and 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.

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