Molecular architecture of the Jumonji C family histone demethylase KDM5B

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

DOI

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

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.

OriginalsprogEngelsk
Artikelnummer4019
TidsskriftScientific Reports
Vol/bind9
ISSN2045-2322
DOI
StatusUdgivet - mar. 2019

Se relationer på Aarhus Universitet Citationsformater

ID: 147634020