DAXX adds a de novo H3.3K9me3 deposition pathway to the histone chaperone network

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

DAXX adds a de novo H3.3K9me3 deposition pathway to the histone chaperone network. / Carraro, Massimo; Hendriks, Ivo A.; Hammond, Colin M.; Solis-Mezarino, Victor; Völker-Albert, Moritz; Elsborg, Jonas D.; Weisser, Melanie B.; Spanos, Christos; Montoya, Guillermo; Rappsilber, Juri; Imhof, Axel; Nielsen, Michael L.; Groth, Anja.

In: Molecular Cell, Vol. 83, No. 7, 2023, p. 1075-1092.e9.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Carraro, M, Hendriks, IA, Hammond, CM, Solis-Mezarino, V, Völker-Albert, M, Elsborg, JD, Weisser, MB, Spanos, C, Montoya, G, Rappsilber, J, Imhof, A, Nielsen, ML & Groth, A 2023, 'DAXX adds a de novo H3.3K9me3 deposition pathway to the histone chaperone network', Molecular Cell, vol. 83, no. 7, pp. 1075-1092.e9. https://doi.org/10.1016/j.molcel.2023.02.009

APA

Carraro, M., Hendriks, I. A., Hammond, C. M., Solis-Mezarino, V., Völker-Albert, M., Elsborg, J. D., Weisser, M. B., Spanos, C., Montoya, G., Rappsilber, J., Imhof, A., Nielsen, M. L., & Groth, A. (2023). DAXX adds a de novo H3.3K9me3 deposition pathway to the histone chaperone network. Molecular Cell, 83(7), 1075-1092.e9. https://doi.org/10.1016/j.molcel.2023.02.009

Vancouver

Carraro M, Hendriks IA, Hammond CM, Solis-Mezarino V, Völker-Albert M, Elsborg JD et al. DAXX adds a de novo H3.3K9me3 deposition pathway to the histone chaperone network. Molecular Cell. 2023;83(7):1075-1092.e9. https://doi.org/10.1016/j.molcel.2023.02.009

Author

Carraro, Massimo ; Hendriks, Ivo A. ; Hammond, Colin M. ; Solis-Mezarino, Victor ; Völker-Albert, Moritz ; Elsborg, Jonas D. ; Weisser, Melanie B. ; Spanos, Christos ; Montoya, Guillermo ; Rappsilber, Juri ; Imhof, Axel ; Nielsen, Michael L. ; Groth, Anja. / DAXX adds a de novo H3.3K9me3 deposition pathway to the histone chaperone network. In: Molecular Cell. 2023 ; Vol. 83, No. 7. pp. 1075-1092.e9.

Bibtex

@article{c1ec9b38cafe4d699039584c9a5375b0,
title = "DAXX adds a de novo H3.3K9me3 deposition pathway to the histone chaperone network",
abstract = "A multitude of histone chaperones are required to support histones from their biosynthesis until DNA deposition. They cooperate through the formation of histone co-chaperone complexes, but the crosstalk between nucleosome assembly pathways remains enigmatic. Using exploratory interactomics, we define the interplay between human histone H3–H4 chaperones in the histone chaperone network. We identify previously uncharacterized histone-dependent complexes and predict the structure of the ASF1 and SPT2 co-chaperone complex, expanding the role of ASF1 in histone dynamics. We show that DAXX provides a unique functionality to the histone chaperone network, recruiting histone methyltransferases to promote H3K9me3 catalysis on new histone H3.3–H4 prior to deposition onto DNA. Hereby, DAXX provides a molecular mechanism for de novo H3K9me3 deposition and heterochromatin assembly. Collectively, our findings provide a framework for understanding how cells orchestrate histone supply and employ targeted deposition of modified histones to underpin specialized chromatin states.",
keywords = "ASF1, DAXX, epigenetic, gene silencing, heterochromatin, histone chaperone, HJURP, NASP, nucleosome assembly, protein network, proteomics",
author = "Massimo Carraro and Hendriks, {Ivo A.} and Hammond, {Colin M.} and Victor Solis-Mezarino and Moritz V{\"o}lker-Albert and Elsborg, {Jonas D.} and Weisser, {Melanie B.} and Christos Spanos and Guillermo Montoya and Juri Rappsilber and Axel Imhof and Nielsen, {Michael L.} and Anja Groth",
note = "Publisher Copyright: {\textcopyright} 2023 The Author(s)",
year = "2023",
doi = "10.1016/j.molcel.2023.02.009",
language = "English",
volume = "83",
pages = "1075--1092.e9",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "7",

}

RIS

TY - JOUR

T1 - DAXX adds a de novo H3.3K9me3 deposition pathway to the histone chaperone network

AU - Carraro, Massimo

AU - Hendriks, Ivo A.

AU - Hammond, Colin M.

AU - Solis-Mezarino, Victor

AU - Völker-Albert, Moritz

AU - Elsborg, Jonas D.

AU - Weisser, Melanie B.

AU - Spanos, Christos

AU - Montoya, Guillermo

AU - Rappsilber, Juri

AU - Imhof, Axel

AU - Nielsen, Michael L.

AU - Groth, Anja

N1 - Publisher Copyright: © 2023 The Author(s)

PY - 2023

Y1 - 2023

N2 - A multitude of histone chaperones are required to support histones from their biosynthesis until DNA deposition. They cooperate through the formation of histone co-chaperone complexes, but the crosstalk between nucleosome assembly pathways remains enigmatic. Using exploratory interactomics, we define the interplay between human histone H3–H4 chaperones in the histone chaperone network. We identify previously uncharacterized histone-dependent complexes and predict the structure of the ASF1 and SPT2 co-chaperone complex, expanding the role of ASF1 in histone dynamics. We show that DAXX provides a unique functionality to the histone chaperone network, recruiting histone methyltransferases to promote H3K9me3 catalysis on new histone H3.3–H4 prior to deposition onto DNA. Hereby, DAXX provides a molecular mechanism for de novo H3K9me3 deposition and heterochromatin assembly. Collectively, our findings provide a framework for understanding how cells orchestrate histone supply and employ targeted deposition of modified histones to underpin specialized chromatin states.

AB - A multitude of histone chaperones are required to support histones from their biosynthesis until DNA deposition. They cooperate through the formation of histone co-chaperone complexes, but the crosstalk between nucleosome assembly pathways remains enigmatic. Using exploratory interactomics, we define the interplay between human histone H3–H4 chaperones in the histone chaperone network. We identify previously uncharacterized histone-dependent complexes and predict the structure of the ASF1 and SPT2 co-chaperone complex, expanding the role of ASF1 in histone dynamics. We show that DAXX provides a unique functionality to the histone chaperone network, recruiting histone methyltransferases to promote H3K9me3 catalysis on new histone H3.3–H4 prior to deposition onto DNA. Hereby, DAXX provides a molecular mechanism for de novo H3K9me3 deposition and heterochromatin assembly. Collectively, our findings provide a framework for understanding how cells orchestrate histone supply and employ targeted deposition of modified histones to underpin specialized chromatin states.

KW - ASF1

KW - DAXX

KW - epigenetic

KW - gene silencing

KW - heterochromatin

KW - histone chaperone

KW - HJURP

KW - NASP

KW - nucleosome assembly

KW - protein network

KW - proteomics

U2 - 10.1016/j.molcel.2023.02.009

DO - 10.1016/j.molcel.2023.02.009

M3 - Journal article

C2 - 36868228

AN - SCOPUS:85151391623

VL - 83

SP - 1075-1092.e9

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 7

ER -

ID: 342094444