Electron microscopy analysis of ATP-independent nucleosome unfolding by FACT.
Adenosine Triphosphate
/ chemistry
DNA-Binding Proteins
/ chemistry
High Mobility Group Proteins
/ chemistry
Humans
Microscopy, Electron, Transmission
Nucleosomes
/ chemistry
Protein Folding
Saccharomyces cerevisiae
/ genetics
Saccharomyces cerevisiae Proteins
/ chemistry
Transcriptional Elongation Factors
/ chemistry
Journal
Communications biology
ISSN: 2399-3642
Titre abrégé: Commun Biol
Pays: England
ID NLM: 101719179
Informations de publication
Date de publication:
10 01 2022
10 01 2022
Historique:
received:
17
08
2021
accepted:
02
12
2021
entrez:
11
1
2022
pubmed:
12
1
2022
medline:
19
2
2022
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 35013515
doi: 10.1038/s42003-021-02948-8
pii: 10.1038/s42003-021-02948-8
pmc: PMC8748794
doi:
Substances chimiques
DNA-Binding Proteins
0
FACT protein, S cerevisiae
0
High Mobility Group Proteins
0
Nucleosomes
0
SSRP1 protein, human
0
Saccharomyces cerevisiae Proteins
0
Transcriptional Elongation Factors
0
Adenosine Triphosphate
8L70Q75FXE
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM119398
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM064649
Pays : United States
Organisme : Russian Science Foundation (RSF)
ID : 19-74-30003
Informations de copyright
© 2022. The Author(s).
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