Expression, purification and characterization of the human MTA2-RBBP7 complex

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Expression, purification and characterization of the human MTA2-RBBP7 complex. / Brasen, Christoffer; Dorosz, Jerzy; Wiuf, Anders; Boesen, Thomas; Mirza, Osman; Gajhede, Michael.

In: Biochimica et biophysica acta, Vol. 1865, No. 5, 04.02.2017, p. 531-538.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Brasen, C, Dorosz, J, Wiuf, A, Boesen, T, Mirza, O & Gajhede, M 2017, 'Expression, purification and characterization of the human MTA2-RBBP7 complex', Biochimica et biophysica acta, vol. 1865, no. 5, pp. 531-538. https://doi.org/10.1016/j.bbapap.2017.02.002

APA

Brasen, C., Dorosz, J., Wiuf, A., Boesen, T., Mirza, O., & Gajhede, M. (2017). Expression, purification and characterization of the human MTA2-RBBP7 complex. Biochimica et biophysica acta, 1865(5), 531-538. https://doi.org/10.1016/j.bbapap.2017.02.002

Vancouver

Brasen C, Dorosz J, Wiuf A, Boesen T, Mirza O, Gajhede M. Expression, purification and characterization of the human MTA2-RBBP7 complex. Biochimica et biophysica acta. 2017 Feb 4;1865(5):531-538. https://doi.org/10.1016/j.bbapap.2017.02.002

Author

Brasen, Christoffer ; Dorosz, Jerzy ; Wiuf, Anders ; Boesen, Thomas ; Mirza, Osman ; Gajhede, Michael. / Expression, purification and characterization of the human MTA2-RBBP7 complex. In: Biochimica et biophysica acta. 2017 ; Vol. 1865, No. 5. pp. 531-538.

Bibtex

@article{cb465fe3ca0f489c863d9e48b57f0096,
title = "Expression, purification and characterization of the human MTA2-RBBP7 complex",
abstract = "The repressive Nucleosome Remodeling and histone Deacetylation (NuRD) complex remodels the chromatin structure by coupling ATP-dependent remodeling activity with histone deacetylase function and plays important roles in regulating gene transcription, DNA damage repair and chromatin assembly. The complex is composed of six subunits: Metastasis Associated proteins MTA1/2/3 initially recruit histone chaperones RBBP4/7 followed by the histone deacetylases HDAC1/2 forming a core complex. Further association of the CpG-binding protein MBD2/3, p66α/β and the ATP-dependent helicase CDH3/4 constitutes the NuRD complex. Recent structural studies on truncated human proteins or orthologous have revealed that the stoichiometry of the MTA1-RBBP4 complex is 2:4. This study reports expression and purification of the intact human MTA2-RBBP7 complex using HEK293F cells as expression system. In analogy with findings on the Drosophila NuRD complex, we find that also the human MTA-RBBP can be isolated in vitro. Taken together with previous findings this suggests, that MTA-RBBP is a stable complex, with a central role in the initial assembly of the human NuRD complex. Refined 3D volumes of the complex generated from negative stain electron microscopy (EM) data reveals an elongated architecture that is capable of hinge like motion around the center of the particle.",
keywords = "Journal Article",
author = "Christoffer Brasen and Jerzy Dorosz and Anders Wiuf and Thomas Boesen and Osman Mirza and Michael Gajhede",
note = "Copyright {\circledC} 2017 Elsevier B.V. All rights reserved.",
year = "2017",
month = "2",
day = "4",
doi = "10.1016/j.bbapap.2017.02.002",
language = "English",
volume = "1865",
pages = "531--538",
journal = "B B A - General Subjects",
issn = "0304-4165",
publisher = "Elsevier",
number = "5",

}

RIS

TY - JOUR

T1 - Expression, purification and characterization of the human MTA2-RBBP7 complex

AU - Brasen, Christoffer

AU - Dorosz, Jerzy

AU - Wiuf, Anders

AU - Boesen, Thomas

AU - Mirza, Osman

AU - Gajhede, Michael

N1 - Copyright © 2017 Elsevier B.V. All rights reserved.

PY - 2017/2/4

Y1 - 2017/2/4

N2 - The repressive Nucleosome Remodeling and histone Deacetylation (NuRD) complex remodels the chromatin structure by coupling ATP-dependent remodeling activity with histone deacetylase function and plays important roles in regulating gene transcription, DNA damage repair and chromatin assembly. The complex is composed of six subunits: Metastasis Associated proteins MTA1/2/3 initially recruit histone chaperones RBBP4/7 followed by the histone deacetylases HDAC1/2 forming a core complex. Further association of the CpG-binding protein MBD2/3, p66α/β and the ATP-dependent helicase CDH3/4 constitutes the NuRD complex. Recent structural studies on truncated human proteins or orthologous have revealed that the stoichiometry of the MTA1-RBBP4 complex is 2:4. This study reports expression and purification of the intact human MTA2-RBBP7 complex using HEK293F cells as expression system. In analogy with findings on the Drosophila NuRD complex, we find that also the human MTA-RBBP can be isolated in vitro. Taken together with previous findings this suggests, that MTA-RBBP is a stable complex, with a central role in the initial assembly of the human NuRD complex. Refined 3D volumes of the complex generated from negative stain electron microscopy (EM) data reveals an elongated architecture that is capable of hinge like motion around the center of the particle.

AB - The repressive Nucleosome Remodeling and histone Deacetylation (NuRD) complex remodels the chromatin structure by coupling ATP-dependent remodeling activity with histone deacetylase function and plays important roles in regulating gene transcription, DNA damage repair and chromatin assembly. The complex is composed of six subunits: Metastasis Associated proteins MTA1/2/3 initially recruit histone chaperones RBBP4/7 followed by the histone deacetylases HDAC1/2 forming a core complex. Further association of the CpG-binding protein MBD2/3, p66α/β and the ATP-dependent helicase CDH3/4 constitutes the NuRD complex. Recent structural studies on truncated human proteins or orthologous have revealed that the stoichiometry of the MTA1-RBBP4 complex is 2:4. This study reports expression and purification of the intact human MTA2-RBBP7 complex using HEK293F cells as expression system. In analogy with findings on the Drosophila NuRD complex, we find that also the human MTA-RBBP can be isolated in vitro. Taken together with previous findings this suggests, that MTA-RBBP is a stable complex, with a central role in the initial assembly of the human NuRD complex. Refined 3D volumes of the complex generated from negative stain electron microscopy (EM) data reveals an elongated architecture that is capable of hinge like motion around the center of the particle.

KW - Journal Article

U2 - 10.1016/j.bbapap.2017.02.002

DO - 10.1016/j.bbapap.2017.02.002

M3 - Journal article

C2 - 28179136

VL - 1865

SP - 531

EP - 538

JO - B B A - General Subjects

JF - B B A - General Subjects

SN - 0304-4165

IS - 5

ER -

ID: 174424394