+検索条件
-Structure paper
タイトル | Structure of the Hir histone chaperone complex. |
---|---|
ジャーナル・号・ページ | Mol Cell, Vol. 84, Issue 14, Page 2601-2617.e12, Year 2024 |
掲載日 | 2024年7月25日 |
著者 | Hee Jong Kim / Mary R Szurgot / Trevor van Eeuwen / M Daniel Ricketts / Pratik Basnet / Athena L Zhang / Austin Vogt / Samah Sharmin / Craig D Kaplan / Benjamin A Garcia / Ronen Marmorstein / Kenji Murakami / |
PubMed 要旨 | The evolutionarily conserved HIRA/Hir histone chaperone complex and ASF1a/Asf1 co-chaperone cooperate to deposit histone (H3/H4) tetramers on DNA for replication-independent chromatin assembly. The ...The evolutionarily conserved HIRA/Hir histone chaperone complex and ASF1a/Asf1 co-chaperone cooperate to deposit histone (H3/H4) tetramers on DNA for replication-independent chromatin assembly. The molecular architecture of the HIRA/Hir complex and its mode of histone deposition have remained unknown. Here, we report the cryo-EM structure of the S. cerevisiae Hir complex with Asf1/H3/H4 at 2.9-6.8 Å resolution. We find that the Hir complex forms an arc-shaped dimer with a Hir1/Hir2/Hir3/Hpc2 stoichiometry of 2/4/2/4. The core of the complex containing two Hir1/Hir2/Hir2 trimers and N-terminal segments of Hir3 forms a central cavity containing two copies of Hpc2, with one engaged by Asf1/H3/H4, in a suitable position to accommodate a histone (H3/H4) tetramer, while the C-terminal segments of Hir3 harbor nucleic acid binding activity to wrap DNA around the Hpc2-assisted histone tetramer. The structure suggests a model for how the Hir/Asf1 complex promotes the formation of histone tetramers for their subsequent deposition onto DNA. |
リンク | Mol Cell / PubMed:38925115 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.96 - 12 Å |
構造データ | EMDB-40006: Hir complex core EMDB-40029: Hir3 Arm/Tail, Hir2 WD40, Hpc2 C-term EMDB-40030, PDB-8ghm: EMDB-40037: Composite map of the Hir complex with Asf1/H3/H4 EMDB-40078, PDB-8gix: |
化合物 | ChemComp-TCE: |
由来 |
|
キーワード | CHAPERONE / Histone / Complex / Replication-Independent / subunit |