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Molecular architecture of the Jumonji C family histone demethylase KDM5B

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  • Jerzy Dorosz, University of Copenhagen
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  • Line Hyltoft Kristensen, University of Copenhagen
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  • Nanda G. Aduri, University of Copenhagen
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  • Osman Mirza, University of Copenhagen
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  • Rikke Lousen, University of Copenhagen
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  • Saskia Bucciarelli, University of Copenhagen
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  • Ved Mehta, University of Copenhagen
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  • Selene Sellés-Baiget, University of Copenhagen
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  • Sara Marie Øie Solbak, University of Copenhagen
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  • Anders Bach, University of Copenhagen
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  • Pablo Mesa, University of Copenhagen
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  • Pablo Alcon Hernandez, University of Copenhagen
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  • Guillermo Montoya, University of Copenhagen
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  • Tam T.T.N. Nguyen, University of Copenhagen
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  • Kasper D. Rand, University of Copenhagen
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  • Thomas Boesen
  • Michael Gajhede, University of Copenhagen

The full length human histone 3 lysine 4 demethylase KDM5B (PLU-1/Jarid1B) has been studied using Hydrogen/Deuterium exchange mass spectrometry, homology modelling, sequence analysis, small angle X-ray scattering and electron microscopy. This first structure on an intact multi-domain Jumonji histone demethylase reveal that the so-called PLU region, in the central region of KDM5B, has a curved α-helical three-dimensional structure, that acts as a rigid linker between the catalytic core and a region comprising four α-helices, a loop comprising the PHD2 domain, two large intrinsically disordered loops and the PHD3 domain in close proximity. The dumbbell shaped and curved KDM5B architecture observed by electron microscopy is complementary to the nucleosome surface and has a striking overall similarity to that of the functionally related KDM1A/CoREST complex. This could suggest that there are similarities between the demethylation mechanisms employed by the two histone 3 lysine 4 demethylases at the molecular level.

Original languageEnglish
Article number4019
JournalScientific Reports
Volume9
Issue1
Number of pages13
ISSN2045-2322
DOIs
Publication statusPublished - Mar 2019

    Research areas

  • BINDING, CRYSTAL-STRUCTURE, DNA, H3K4, MECHANISMS, PROTEINS, RECOGNITION, RECOMBINANT HISTONES, SMALL-ANGLE SCATTERING, X-RAY-SCATTERING

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