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Cells, volume 11, issue 18, pages 2837

H2A-H2B Histone Dimer Plasticity and Its Functional Implications

Kniazeva Anastasiia S ¹

Armeev Grigoriy A ¹

Shaytan Alexey K ¹

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Department of Biology, Lomonosov Moscow State University, 119234 Moscow, Russia |

Publication type: Journal Article

Publication date: 2022-09-12

Multidisciplinary Digital Publishing Institute (MDPI)

Journal: Cells

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Impact factor: 6

ISSN: 20734409

DOI: 10.3390/cells11182837

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General Medicine

Abstract

The protein core of the nucleosome is composed of an H3-H4 histone tetramer and two H2A-H2B histone dimers. The tetramer organizes the central 60 DNA bp, while H2A-H2B dimers lock the flanking DNA segments. Being positioned at the sides of the nucleosome, H2A-H2B dimers stabilize the overall structure of the nucleosome and modulate its dynamics, such as DNA unwrapping, sliding, etc. Such modulation at the epigenetic level is achieved through post-translational modifications and the incorporation of histone variants. However, the detailed connection between the sequence of H2A-H2B histones and their structure, dynamics and implications for nucleosome functioning remains elusive. In this work, we present a detailed study of H2A-H2B dimer dynamics in the free form and in the context of nucleosomes via atomistic molecular dynamics simulations (based on X. laevis histones). We supplement simulation results by comparative analysis of information in the structural databases. Particularly, we describe a major dynamical mode corresponding to the bending movement of the longest H2A and H2B α-helices. This overall bending dynamics of the H2A-H2B dimer were found to be modulated by its interactions with DNA, H3-H4 tetramer, the presence of DNA twist-defects with nucleosomal DNA and the amino acid sequence of histones. Taken together, our results shed new light on the dynamical mechanisms of nucleosome functioning, such as nucleosome sliding, DNA-unwrapping and their epigenetic modulation.

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Nature Communications	Nature Communications, 1, 33.33% Nature Communications 1 publication, 33.33%
International Journal of Molecular Sciences	International Journal of Molecular Sciences, 1, 33.33% International Journal of Molecular Sciences 1 publication, 33.33%
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Springer Nature	Springer Nature, 1, 33.33% Springer Nature 1 publication, 33.33%
Multidisciplinary Digital Publishing Institute (MDPI)	Multidisciplinary Digital Publishing Institute (MDPI), 1, 33.33% Multidisciplinary Digital Publishing Institute (MDPI) 1 publication, 33.33%
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Kniazeva A. S., Armeev G. A., Shaytan A. K. H2A-H2B Histone Dimer Plasticity and Its Functional Implications // Cells. 2022. Vol. 11. No. 18. p. 2837.

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Kniazeva A. S., Armeev G. A., Shaytan A. K. H2A-H2B Histone Dimer Plasticity and Its Functional Implications // Cells. 2022. Vol. 11. No. 18. p. 2837.

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TY - JOUR

DO - 10.3390/cells11182837

UR - https://doi.org/10.3390%2Fcells11182837

TI - H2A-H2B Histone Dimer Plasticity and Its Functional Implications

T2 - Cells

AU - Kniazeva, Anastasiia S

AU - Armeev, Grigoriy A

AU - Shaytan, Alexey K

PY - 2022

DA - 2022/09/12 00:00:00

PB - Multidisciplinary Digital Publishing Institute (MDPI)

SP - 2837

IS - 18

VL - 11

SN - 2073-4409

ER -

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@article{2022_Kniazeva,

author = {Anastasiia S Kniazeva and Grigoriy A Armeev and Alexey K Shaytan},

title = {H2A-H2B Histone Dimer Plasticity and Its Functional Implications},

journal = {Cells},

year = {2022},

volume = {11},

publisher = {Multidisciplinary Digital Publishing Institute (MDPI)},

month = {sep},

url = {https://doi.org/10.3390%2Fcells11182837},

number = {18},

pages = {2837},

doi = {10.3390/cells11182837}

}

MLA

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Kniazeva, Anastasiia S., et al. “H2A-H2B Histone Dimer Plasticity and Its Functional Implications.” Cells, vol. 11, no. 18, Sep. 2022, p. 2837. https://doi.org/10.3390%2Fcells11182837.

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Publisher

Multidisciplinary Digital Publishing Institute (MDPI)

Journal

Cells

Quartile SCImago

Quartile WOS

Impact factor

ISSN

20734409 (Print)

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Armeev, Grigoriy Alekseevich

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