Dataset Information

Histone modifications associated with the histone chaperone DAXX

ABSTRACT: A multitude of histone chaperones is required to protect histones from their biosynthesis to DNA deposition. They cooperate through the formation of co-chaperone complexes, but the crosstalk between nucleosome assembly pathways is unclear. Using explorative interactomics approaches, we map the organization of the histone H3-H4 chaperones network and define the interplay between histone chaperones systems. We identify and validate a panel of novel histone (PTM) dependent complexes. We show DAXX acts separately from the rest of the network, recruiting heterochromatin factors and promoting lysine 9 tri-methylated new histone H3.3 prior to deposition onto DNA. With its functionality, DAXX provides a molecular mechanism for de novo heterochromatin assembly.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Embryo, Embryonic Stem Cell

SUBMITTER: Victor Solis

LAB HEAD: Anja Groth

PROVIDER: PXD034924 | Pride | 2023-03-06

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	Exp-design_PRIDE-Submission.txt	Txt
	RefXXX_BRIC_DAXX_ATRX1_181220.raw	Raw
	RefXXX_BRIC_DAXX_ATRX2_181220.raw	Raw
	RefXXX_BRIC_DAXX_ATRX3_181220.raw	Raw
	RefXXX_BRIC_DAXX_WT2_181220.raw	Raw

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Publications

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

Carraro Massimo M Hendriks Ivo A IA Hammond Colin M CM Solis-Mezarino Victor V Völker-Albert Moritz M Elsborg Jonas D JD Weisser Melanie B MB Spanos Christos C Montoya Guillermo G Rappsilber Juri J Imhof Axel A Nielsen Michael L ML Groth Anja A

Molecular cell 20230302 7

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 SP ...[more]

PMID: 36868228

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