The histone chaperone Spt6 controls chromatin structure through its conserved N-terminal domain
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F25%3A00639394" target="_blank" >RIV/61388963:_____/25:00639394 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11310/25:10505745
Result on the web
<a href="https://doi.org/10.1016/j.molcel.2025.08.020" target="_blank" >https://doi.org/10.1016/j.molcel.2025.08.020</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.molcel.2025.08.020" target="_blank" >10.1016/j.molcel.2025.08.020</a>
Alternative languages
Result language
angličtina
Original language name
The histone chaperone Spt6 controls chromatin structure through its conserved N-terminal domain
Original language description
The disassembly and reassembly of nucleosomes by histone chaperones is an essential activity during eukaryotic transcription elongation. This highly conserved process maintains chromatin integrity by transiently removing nucleosomes as barriers and then restoring them in the wake of transcription. While transcription elongation requires multiple histone chaperones, there is little understanding of how most of them function and why so many are required. Here, we show that the histone chaperone Spt6 acts through its acidic, intrinsically disordered N-terminal domain (NTD) to bind histones and control chromatin structure. The Spt6 NTD is essential for viability, and its histone-binding activity is conserved between yeast and humans. The essential nature of the Spt6 NTD can be bypassed by changes in another histone chaperone, FACT, revealing a close functional connection between the two. Our results have led to a mechanistic model for dynamic cooperation between multiple histone chaperones during transcription elongation.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
—
OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
<a href="/en/project/GX25-15442X" target="_blank" >GX25-15442X: Disentangling transient interactions in transcription elongation</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Molecular Cell
ISSN
1097-2765
e-ISSN
1097-4164
Volume of the periodical
85
Issue of the periodical within the volume
18
Country of publishing house
US - UNITED STATES
Number of pages
18
Pages from-to
3407-3424
UT code for WoS article
001576687800001
EID of the result in the Scopus database
2-s2.0-105015644983