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The GBAF chromatin remodeling complex binds H3K27ac and mediates enhancer transcription

View ORCID ProfileKirill Jefimov, View ORCID ProfileNicolas Alcaraz, View ORCID ProfileSusan L. Kloet, View ORCID ProfileSigne Värv, Siri Aastedatter Sakya, Christian Dalager Vaagenso, View ORCID ProfileMichiel Vermeulen, View ORCID ProfileRein Aasland, View ORCID Profileand Robin Andersson
doi: https://doi.org/10.1101/445148
Kirill Jefimov
1Department of Biological Sciences, University of Bergen, 5008 Bergen, Norway
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Nicolas Alcaraz
2The Bioinformatics Centre, Department of Biology, University of Copenhagen, 2200 Copenhagen, Denmark
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Susan L. Kloet
3Department of Molecular Biology, Radboud Institute for Molecular Life Sciences, Radboud University Nijmegen, 6525 Nijmegen, The Netherlands
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Signe Värv
4Department of Biosciences, University of Oslo, 0371 Oslo, Norway
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Siri Aastedatter Sakya
1Department of Biological Sciences, University of Bergen, 5008 Bergen, Norway
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Christian Dalager Vaagenso
2The Bioinformatics Centre, Department of Biology, University of Copenhagen, 2200 Copenhagen, Denmark
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Michiel Vermeulen
3Department of Molecular Biology, Radboud Institute for Molecular Life Sciences, Radboud University Nijmegen, 6525 Nijmegen, The Netherlands
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  • For correspondence: michiel.vermeulen@science.ru.nl rein.aasland@ibv.uio.no robin@binf.ku.dk
Rein Aasland
4Department of Biosciences, University of Oslo, 0371 Oslo, Norway
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  • For correspondence: michiel.vermeulen@science.ru.nl rein.aasland@ibv.uio.no robin@binf.ku.dk
and Robin Andersson
2The Bioinformatics Centre, Department of Biology, University of Copenhagen, 2200 Copenhagen, Denmark
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  • For correspondence: michiel.vermeulen@science.ru.nl rein.aasland@ibv.uio.no robin@binf.ku.dk
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Abstract

H3K27ac is associated with regulatory active enhancers, but its exact role in enhancer function remains elusive. Using mass spectrometry-based interaction proteomics, we identified the Super Elongation Complex (SEC) and GBAF, a non-canonical GLTSCR1L- and BRD9-containing SWI/SNF chromatin remodeling complex, to be major interactors of H3K27ac. We systematically characterized the composition of GBAF and the conserved GLTSCR1/1L ‘GiBAF’-domain, which we found to be responsible for GBAF complex formation and GLTSCR1L nuclear localization. Inhibition of the bromodomain of BRD9 revealed interaction between GLTSCR1L and H3K27ac to be BRD9-dependent and led to GLTSCR1L dislocation from its preferred binding sites at H3K27ac-associated enhancers. GLTSCR1L disassociation from chromatin resulted in genome-wide downregulation of enhancer transcription while leaving most mRNA expression levels unchanged, except for reduced mRNA levels from loci topologically linked to affected enhancers. Our results indicate that GBAF is an enhancer-associated chromatin remodeler important for transcriptional and regulatory activity of enhancers.

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Posted October 17, 2018.
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The GBAF chromatin remodeling complex binds H3K27ac and mediates enhancer transcription
Kirill Jefimov, Nicolas Alcaraz, Susan L. Kloet, Signe Värv, Siri Aastedatter Sakya, Christian Dalager Vaagenso, Michiel Vermeulen, Rein Aasland, and Robin Andersson
bioRxiv 445148; doi: https://doi.org/10.1101/445148
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The GBAF chromatin remodeling complex binds H3K27ac and mediates enhancer transcription
Kirill Jefimov, Nicolas Alcaraz, Susan L. Kloet, Signe Värv, Siri Aastedatter Sakya, Christian Dalager Vaagenso, Michiel Vermeulen, Rein Aasland, and Robin Andersson
bioRxiv 445148; doi: https://doi.org/10.1101/445148

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