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Molecular architecture of the Jumonji C family histone demethylase KDM5B.

Abstract：

: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.

journal_name

Sci Rep

journal_title

Scientific reports

authors

Dorosz J,Kristensen LH,Aduri NG,Mirza O,Lousen R,Bucciarelli S,Mehta V,Sellés-Baiget S,Solbak SMØ,Bach A,Mesa P,Hernandez PA,Montoya G,Nguyen TTTN,Rand KD,Boesen T,Gajhede M

doi

10.1038/s41598-019-40573-y

subject

Has Abstract

pub_date

2019-03-11 00:00:00

pages

4019

issue

1

issn

2045-2322

pii

10.1038/s41598-019-40573-y

journal_volume

9

pub_type

杂志文章

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