The histone chaperone Spt6 controls chromatin structure through its conserved N-terminal domain
Identifikátory výsledku
Kód výsledku v 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>
Nalezeny alternativní kódy
RIV/00216208:11310/25:10505745
Výsledek na webu
<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>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
The histone chaperone Spt6 controls chromatin structure through its conserved N-terminal domain
Popis výsledku v původním jazyce
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.
Název v anglickém jazyce
The histone chaperone Spt6 controls chromatin structure through its conserved N-terminal domain
Popis výsledku anglicky
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.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10608 - Biochemistry and molecular biology
Návaznosti výsledku
Projekt
<a href="/cs/project/GX25-15442X" target="_blank" >GX25-15442X: Rozplétání tranzientních interakcí během transkripční elongace</a><br>
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2025
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Molecular Cell
ISSN
1097-2765
e-ISSN
1097-4164
Svazek periodika
85
Číslo periodika v rámci svazku
18
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
18
Strana od-do
3407-3424
Kód UT WoS článku
001576687800001
EID výsledku v databázi Scopus
2-s2.0-105015644983