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TitleMolecular architecture of the Jumonji C family histone demethylase KDM5B.
Journal, issue, pagesSci Rep, Vol. 9, Issue 1, Page 4019, Year 2019
Publish dateMar 11, 2019
AuthorsJerzy Dorosz / Line Hyltoft Kristensen / Nanda G Aduri / Osman Mirza / Rikke Lousen / Saskia Bucciarelli / Ved Mehta / Selene Sellés-Baiget / Sara Marie Øie Solbak / Anders Bach / Pablo Mesa / Pablo Alcon Hernandez / Guillermo Montoya / Tam T T N Nguyen / Kasper D Rand / Thomas Boesen / Michael Gajhede /
PubMed AbstractThe 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- ...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.
External linksSci Rep / PubMed:30858420 / PubMed Central
MethodsSAS (X-ray in house) / EM (single particle)
Resolution27.0 Å
Structure data

SASDE37:
Lysine-specific demethylase 5B, KDM5B, in HEPES buffer
Method: SAXS/SANS

EMDB-3982:
Molecular Architecture of the Jumonji C histone demethylase KDM5B.
Method: EM (single particle) / Resolution: 27.0 Å

Source
  • Homo sapiens (human)

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