Open Access
Communications Biology, volume 5, issue 1, publication number 2
Electron microscopy analysis of ATP-independent nucleosome unfolding by FACT
Sivkina Anastasiia L
1, 2
,
Karlova Maria G.
2
,
Valieva Maria E
2, 3, 4
,
Mccullough Laura L
5
,
Formosa Tim
5
,
Shaytan Alexey K
2, 6
,
Feofanov Alexey V
2, 7
,
Kirpichnikov Mikhail P.
2, 7
,
Sokolova Olga S.
2, 8
,
Studitsky V. M.
1, 2
1
Fox Chase Cancer center, Philadelphia, USA
|
3
Institute for Medical and Human Genetics, Charité-Universitätsmedizin Berlin, Berlin, Germany
|
4
RG Development & Disease, Max Planck Institute for Molecular Genetics, Berlin, Germany
|
5
Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, USA
|
7
Publication type: Journal Article
Publication date: 2022-01-10
Journal:
Communications Biology
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 5.9
ISSN: 23993642
PubMed ID:
35013515
General Biochemistry, Genetics and Molecular Biology
Medicine (miscellaneous)
General Agricultural and Biological Sciences
Abstract
FACT is a histone chaperone that participates in nucleosome removal and reassembly during transcription and replication. We used electron microscopy to study FACT, FACT:Nhp6 and FACT:Nhp6:nucleosome complexes, and found that all complexes adopt broad ranges of configurations, indicating high flexibility. We found unexpectedly that the DNA binding protein Nhp6 also binds to the C-terminal tails of FACT subunits, inducing more open geometries of FACT even in the absence of nucleosomes. Nhp6 therefore supports nucleosome unfolding by altering both the structure of FACT and the properties of nucleosomes. Complexes formed with FACT, Nhp6, and nucleosomes also produced a broad range of structures, revealing a large number of potential intermediates along a proposed unfolding pathway. The data suggest that Nhp6 has multiple roles before and during nucleosome unfolding by FACT, and that the process proceeds through a series of energetically similar intermediate structures, ultimately leading to an extensively unfolded form.
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- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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Sivkina A. L. et al. Electron microscopy analysis of ATP-independent nucleosome unfolding by FACT // Communications Biology. 2022. Vol. 5. No. 1. 2
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Sivkina A. L., Karlova M. G., Valieva M. E., Mccullough L. L., Formosa T., Shaytan A. K., Feofanov A. V., Kirpichnikov M. P., Sokolova O. S., Studitsky V. M. Electron microscopy analysis of ATP-independent nucleosome unfolding by FACT // Communications Biology. 2022. Vol. 5. No. 1. 2
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TY - JOUR
DO - 10.1038/s42003-021-02948-8
UR - https://doi.org/10.1038%2Fs42003-021-02948-8
TI - Electron microscopy analysis of ATP-independent nucleosome unfolding by FACT
T2 - Communications Biology
AU - Sivkina, Anastasiia L
AU - Karlova, Maria G.
AU - Valieva, Maria E
AU - Mccullough, Laura L
AU - Formosa, Tim
AU - Shaytan, Alexey K
AU - Feofanov, Alexey V
AU - Kirpichnikov, Mikhail P.
AU - Sokolova, Olga S.
AU - Studitsky, V. M.
PY - 2022
DA - 2022/01/10 00:00:00
PB - Springer Nature
IS - 1
VL - 5
PMID - 35013515
SN - 2399-3642
ER -
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@article{2022_Sivkina,
author = {Anastasiia L Sivkina and Maria G. Karlova and Maria E Valieva and Laura L Mccullough and Tim Formosa and Alexey K Shaytan and Alexey V Feofanov and Mikhail P. Kirpichnikov and Olga S. Sokolova and V. M. Studitsky},
title = {Electron microscopy analysis of ATP-independent nucleosome unfolding by FACT},
journal = {Communications Biology},
year = {2022},
volume = {5},
publisher = {Springer Nature},
month = {jan},
url = {https://doi.org/10.1038%2Fs42003-021-02948-8},
number = {1},
doi = {10.1038/s42003-021-02948-8}
}