Molecular basis and specificity of H2A.Z-H2B recognition and deposition by the histone chaperone YL1

Chrysa M. Latrick, Martin Marek, Khalid Ouararhni, Christophe Papin, Isabelle Stoll, Maria Ignatyeva, Arnaud Obri, Eric Ennifar, Stefan Dimitrov, Christophe Romier, Ali Hamiche

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

H2A.Z, a widely conserved histone variant, is evicted from chromatin by the histone chaperone ANP32E. However, to date, no deposition chaperone for H2A.Z is known in metazoans. Here, we identify YL1 as a specific H2A.Z-deposition chaperone. The 2.7-Å-resolution crystal structure of the human YL1-H2A.Z-H2B complex shows that YL1 binding, similarly to ANP32E binding, triggers an extension of the H2A.Z αC helix. The interaction with YL1 is, however, more extensive and includes both the extended acidic patch and the entire DNA-binding surface of H2A.Z-H2B. Substitution of only four amino acid residues of H2A is sufficient for the formation of an H2A.Z-like interface specifically recognized by YL1. Collectively, our data reveal the molecular basis of H2A.Z-specific recognition by YL1 and shed light on the mechanism of H2A.Z transfer to the nucleosome by the ATP-dependent chromatin-remodeling complexes SRCAP and P400-TIP60.

Original languageEnglish
Pages (from-to)309-316
Number of pages8
JournalNature Structural and Molecular Biology
Volume23
Issue number4
DOIs
Publication statusPublished - 5 Apr 2016
Externally publishedYes

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Histone Chaperones
Chromatin Assembly and Disassembly
Nucleosomes
Histones
Chromatin
Adenosine Triphosphate
Amino Acids
DNA

ASJC Scopus subject areas

  • Structural Biology
  • Medicine(all)
  • Molecular Biology

Cite this

Molecular basis and specificity of H2A.Z-H2B recognition and deposition by the histone chaperone YL1. / Latrick, Chrysa M.; Marek, Martin; Ouararhni, Khalid; Papin, Christophe; Stoll, Isabelle; Ignatyeva, Maria; Obri, Arnaud; Ennifar, Eric; Dimitrov, Stefan; Romier, Christophe; Hamiche, Ali.

In: Nature Structural and Molecular Biology, Vol. 23, No. 4, 05.04.2016, p. 309-316.

Research output: Contribution to journalArticle

Latrick, CM, Marek, M, Ouararhni, K, Papin, C, Stoll, I, Ignatyeva, M, Obri, A, Ennifar, E, Dimitrov, S, Romier, C & Hamiche, A 2016, 'Molecular basis and specificity of H2A.Z-H2B recognition and deposition by the histone chaperone YL1', Nature Structural and Molecular Biology, vol. 23, no. 4, pp. 309-316. https://doi.org/10.1038/nsmb.3189
Latrick, Chrysa M. ; Marek, Martin ; Ouararhni, Khalid ; Papin, Christophe ; Stoll, Isabelle ; Ignatyeva, Maria ; Obri, Arnaud ; Ennifar, Eric ; Dimitrov, Stefan ; Romier, Christophe ; Hamiche, Ali. / Molecular basis and specificity of H2A.Z-H2B recognition and deposition by the histone chaperone YL1. In: Nature Structural and Molecular Biology. 2016 ; Vol. 23, No. 4. pp. 309-316.
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