TY - JOUR
T1 - The Histone Chaperones SET/TAF-1β and NPM1 Exhibit Conserved Functionality in Nucleosome Remodeling and Histone Eviction in a Cytochrome c-Dependent Manner
AU - Buzón, Pedro
AU - Velázquez-Cruz, Alejandro
AU - Corrales-Guerrero, Laura
AU - Díaz-Quintana, Antonio
AU - Díaz-Moreno, Irene
AU - Roos, Wouter H.
N1 - Funding Information:
This work was supported by a Vidi grant of NWO (to W.H.R.), an FPU predoctoral contract of the Spanish Ministry of Education, Culture and Sports (FPU016/01513, to A.V.C.), a postdoctoral contract of the European Social Fund (PAIDI‐DOCTOR 2020 DOC_00796, to L.C.G.), a travel grant of EMBO (Short‐Term Fellowship 8541, to A.V.C.) and a travel grant of the European ARBRE‐Mobieu consortium (COST Action CA15126, to A.D.Q.). The authors are grateful to the Spanish Ministry of Science and Innovation (PGC 2018‐096049‐ BI00 and PID2021‐126663NB‐100), the Regional Government of Andalusia (BIO198, US‐1254317 US/JUNTA/FEDER,UE, P18‐FR‐3487 and P18–HO‐4091) and the Ramón Areces Foundation (2021‐2024). The authors thank Gonzalo Pérez‐Mejías and Manuel Angulo for their assistance in the NMR measurements at CITIUS (University of Seville). The authors also thank Gijs Wuite, Rifka Vlijm, Katiuska González‐Arzola, and Jonathan Martínez‐Fábregas for critical feedback on the manuscript and discussions.
Publisher Copyright:
© 2023 The Authors. Advanced Science published by Wiley-VCH GmbH.
PY - 2023/10/17
Y1 - 2023/10/17
N2 - Chromatin homeostasis mediates essential processes in eukaryotes, where histone chaperones have emerged as major regulatory factors during DNA replication, repair, and transcription. The dynamic nature of these processes, however, has severely impeded their characterization at the molecular level. Here, fluorescence optical tweezers are applied to follow histone chaperone dynamics in real time. The molecular action of SET/template-activating factor-Iβ and nucleophosmin 1—representing the two most common histone chaperone folds—are examined using both nucleosomes and isolated histones. It is shown that these chaperones present binding specificity for fully dismantled nucleosomes and are able to recognize and disrupt non-native histone-DNA interactions. Furthermore, the histone eviction process and its modulation by cytochrome c are scrutinized. This approach shows that despite the different structures of these chaperones, they present conserved modes of action mediating nucleosome remodeling.
AB - Chromatin homeostasis mediates essential processes in eukaryotes, where histone chaperones have emerged as major regulatory factors during DNA replication, repair, and transcription. The dynamic nature of these processes, however, has severely impeded their characterization at the molecular level. Here, fluorescence optical tweezers are applied to follow histone chaperone dynamics in real time. The molecular action of SET/template-activating factor-Iβ and nucleophosmin 1—representing the two most common histone chaperone folds—are examined using both nucleosomes and isolated histones. It is shown that these chaperones present binding specificity for fully dismantled nucleosomes and are able to recognize and disrupt non-native histone-DNA interactions. Furthermore, the histone eviction process and its modulation by cytochrome c are scrutinized. This approach shows that despite the different structures of these chaperones, they present conserved modes of action mediating nucleosome remodeling.
KW - fluorescence microscopy
KW - nucleophosmin 1
KW - optical tweezers
KW - SET/template-activating factor-Iβ
KW - single-molecule methods
UR - http://www.scopus.com/inward/record.url?scp=85166934569&partnerID=8YFLogxK
U2 - 10.1002/advs.202301859
DO - 10.1002/advs.202301859
M3 - Article
AN - SCOPUS:85166934569
SN - 2198-3844
VL - 10
JO - Advanced science
JF - Advanced science
IS - 29
M1 - 2301859
ER -