Format

Send to

Choose Destination
Nat Struct Mol Biol. 2016 Apr;23(4):309-16. doi: 10.1038/nsmb.3189. Epub 2016 Mar 14.

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

Author information

1
Equipe Labélisée Ligue Contre le Cancer, Département de Génomique Fonctionnelle et Cancer, Institut de Génétique et Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France.
2
Département de Biologie Structurale Intégrative, IGBMC, Illkirch, France.
3
Architecture et Réactivité de l'ARN, Université de Strasbourg, Institut de Biologie Moléculaire et Cellulaire du CNRS, Strasbourg, France.
4
Département Différenciation et Transformation Cellulaire, Institut Albert Bonniot, Grenoble, France.

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.

PMID:
26974126
DOI:
10.1038/nsmb.3189
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Nature Publishing Group
Loading ...
Support Center