DAXX adds a de novo H3.3K9me3 deposition pathway to the histone chaperone network
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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.
I: Molecular Cell, Bind 83, Nr. 7, 2023, s. 1075-1092.e9.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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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