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  H3.Y discriminates between HIRA and DAXX chaperone complexes and reveals unexpected insights into human DAXX-H3.3-H4 binding and deposition requirements

Zink, L.-M., Delbarre, E., Eberl, H. C., Keilhauer, E. C., Boenisch, C., Puenzeler, S., et al. (2017). H3.Y discriminates between HIRA and DAXX chaperone complexes and reveals unexpected insights into human DAXX-H3.3-H4 binding and deposition requirements. Nucleic Acids Research (London), 45(10), 5691-5706. doi:10.1093/nar/gkx131.

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 Creators:
Zink, Lisa-Maria1, Author
Delbarre, Erwan1, Author
Eberl, H. Christian2, Author              
Keilhauer, Eva C.2, Author              
Boenisch, Clemens1, Author
Puenzeler, Sebastian1, Author
Bartkuhn, Marek1, Author
Collas, Philippe1, Author
Mann, Matthias2, Author              
Hake, Sandra B.1, Author
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1external, ou_persistent22              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              

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Free keywords: HISTONE VARIANT H3.3; EMBRYONIC STEM-CELLS; DNA-SYNTHESIS; IN-VIVO; NUCLEOSOME; CHROMATIN; IDENTIFICATION; REPLICATION; ENRICHMENT; PROTEOMICSBiochemistry & Molecular Biology;
 Abstract: Histone chaperones prevent promiscuous histone interactions before chromatin assembly. They guarantee faithful deposition of canonical histones and functionally specialized histone variants into chromatin in a spatial-and temporally-restricted manner. Here, we identify the binding partners of the primate-specific and H3.3-related histone variant H3.Y using several quantitative mass spectrometry approaches, and biochemical and cell biological assays. We find the HIRA, but not the DAXX/ATRX, complex to recognize H3.Y, explaining its presence in transcriptionally active euchromatic regions. Accordingly, H3.Y nucleosomes are enriched in the transcription-promoting FACT complex and depleted of repressive post-translational histone modifications. H3.Y mutational gain-of-function screens reveal an unexpected combinatorial amino acid sequence requirement for histone H3.3 interaction with DAXX but not HIRA, and for H3.3 recruitment to PML nuclear bodies. We demonstrate the importance and necessity of specific H3.3 core and C-terminal amino acids in discriminating between distinct chaperone complexes. Further, chromatin immunoprecipitation sequencing experiments reveal that in contrast to euchromatic HIRA-dependent deposition sites, human DAXX/ATRX-dependent regions of histone H3 variant incorporation are enriched in heterochromatic H3K9me3 and simple repeat sequences. These data demonstrate that H3.Y's unique amino acids allow a functional distinction between HIRA and DAXX binding and its consequent deposition into open chromatin.

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Language(s): eng - English
 Dates: 2017-02-212017-06
 Publication Status: Published in print
 Pages: 16
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000402510700023
DOI: 10.1093/nar/gkx131
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Title: Nucleic Acids Research (London)
  Other : Nucleic Acids Res
Source Genre: Journal
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Publ. Info: Oxford : Oxford University Press
Pages: - Volume / Issue: 45 (10) Sequence Number: - Start / End Page: 5691 - 5706 Identifier: ISSN: 0305-1048
CoNE: https://pure.mpg.de/cone/journals/resource/110992357379342