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Molecular architecture of the Jumonji C family histone demethylase KDM5B

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Molecular architecture of the Jumonji C family histone demethylase KDM5B. / Dorosz, Jerzy; Kristensen, Line Hyltoft; Aduri, Nanda G. et al.

In: Scientific Reports, Vol. 9, No. 1, 4019, 03.2019.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Harvard

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 2019, 'Molecular architecture of the Jumonji C family histone demethylase KDM5B', Scientific Reports, vol. 9, no. 1, 4019. https://doi.org/10.1038/s41598-019-40573-y

APA

Dorosz, J., Kristensen, L. H., Aduri, N. G., Mirza, O., Lousen, R., Bucciarelli, S., Mehta, V., Sellés-Baiget, S., Solbak, S. M. Ø., Bach, A., Mesa, P., Hernandez, P. A., Montoya, G., Nguyen, T. T. T. N., Rand, K. D., Boesen, T., & Gajhede, M. (2019). Molecular architecture of the Jumonji C family histone demethylase KDM5B. Scientific Reports, 9(1), [4019]. https://doi.org/10.1038/s41598-019-40573-y

CBE

Dorosz J, Kristensen LH, Aduri NG, Mirza O, Lousen R, Bucciarelli S, Mehta V, Sellés-Baiget S, Solbak SMØ, Bach A, et al. 2019. Molecular architecture of the Jumonji C family histone demethylase KDM5B. Scientific Reports. 9(1):Article 4019. https://doi.org/10.1038/s41598-019-40573-y

MLA

Dorosz, Jerzy et al. "Molecular architecture of the Jumonji C family histone demethylase KDM5B". Scientific Reports. 2019. 9(1). https://doi.org/10.1038/s41598-019-40573-y

Vancouver

Dorosz J, Kristensen LH, Aduri NG, Mirza O, Lousen R, Bucciarelli S et al. Molecular architecture of the Jumonji C family histone demethylase KDM5B. Scientific Reports. 2019 Mar;9(1):4019. doi: 10.1038/s41598-019-40573-y

Author

Dorosz, Jerzy ; Kristensen, Line Hyltoft ; Aduri, Nanda G. et al. / Molecular architecture of the Jumonji C family histone demethylase KDM5B. In: Scientific Reports. 2019 ; Vol. 9, No. 1.

Bibtex

@article{b6059fcf2af04c67a041d10d723a47f6,
title = "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.",
keywords = "BINDING, CRYSTAL-STRUCTURE, DNA, H3K4, MECHANISMS, PROTEINS, RECOGNITION, RECOMBINANT HISTONES, SMALL-ANGLE SCATTERING, X-RAY-SCATTERING",
author = "Jerzy Dorosz and Kristensen, {Line Hyltoft} and Aduri, {Nanda G.} and Osman Mirza and Rikke Lousen and Saskia Bucciarelli and Ved Mehta and Selene Sell{\'e}s-Baiget and Solbak, {Sara Marie {\O}ie} and Anders Bach and Pablo Mesa and Hernandez, {Pablo Alcon} and Guillermo Montoya and Nguyen, {Tam T.T.N.} and Rand, {Kasper D.} and Thomas Boesen and Michael Gajhede",
year = "2019",
month = mar,
doi = "10.1038/s41598-019-40573-y",
language = "English",
volume = "9",
journal = "Scientific Reports",
issn = "2045-2322",
publisher = "Nature Publishing Group",
number = "1",

}

RIS

TY - JOUR

T1 - Molecular architecture of the Jumonji C family histone demethylase KDM5B

AU - Dorosz, Jerzy

AU - Kristensen, Line Hyltoft

AU - Aduri, Nanda G.

AU - Mirza, Osman

AU - Lousen, Rikke

AU - Bucciarelli, Saskia

AU - Mehta, Ved

AU - Sellés-Baiget, Selene

AU - Solbak, Sara Marie Øie

AU - Bach, Anders

AU - Mesa, Pablo

AU - Hernandez, Pablo Alcon

AU - Montoya, Guillermo

AU - Nguyen, Tam T.T.N.

AU - Rand, Kasper D.

AU - Boesen, Thomas

AU - Gajhede, Michael

PY - 2019/3

Y1 - 2019/3

N2 - 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.

AB - 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.

KW - BINDING

KW - CRYSTAL-STRUCTURE

KW - DNA

KW - H3K4

KW - MECHANISMS

KW - PROTEINS

KW - RECOGNITION

KW - RECOMBINANT HISTONES

KW - SMALL-ANGLE SCATTERING

KW - X-RAY-SCATTERING

UR - http://www.scopus.com/inward/record.url?scp=85062766423&partnerID=8YFLogxK

U2 - 10.1038/s41598-019-40573-y

DO - 10.1038/s41598-019-40573-y

M3 - Journal article

C2 - 30858420

AN - SCOPUS:85062766423

VL - 9

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

IS - 1

M1 - 4019

ER -