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Structural basis of nucleosome assembly by the Abo1 AAA+ ATPase histone chaperone

DOI: 10.1038/s41467-019-13743-9 DOI Help

Authors: Carol Cho (Korea Advanced Institute of Science and Technology (KAIST)) , Juwon Jang (Korea Advanced Institute of Science and Technology (KAIST)) , Yujin Kang (Ulsan National Institute of Science and Technology) , Hiroki Watanabe (National Institutes of Natural Sciences, Japan) , Takayuki Uchihashi (National Institutes of Natural Sciences, Japan; Nagoya University) , Seung Joong Kim (Korea Advanced Institute of Science and Technology (KAIST)) , Koichi Kato (National Institutes of Natural Sciences, Japan; Nagoya City University) , Ja Yil Lee (Ulsan National Institute of Science and Technology) , Ji-Joon Song (Korea Advanced Institute of Science and Technology (KAIST))
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 10

State: Published (Approved)
Published: December 2019
Diamond Proposal Number(s): 22985

Open Access Open Access

Abstract: The fundamental unit of chromatin, the nucleosome, is an intricate structure that requires histone chaperones for assembly. ATAD2 AAA+ ATPases are a family of histone chaperones that regulate nucleosome density and chromatin dynamics. Here, we demonstrate that the fission yeast ATAD2 homolog, Abo1, deposits histone H3–H4 onto DNA in an ATP-hydrolysis-dependent manner by in vitro reconstitution and single-tethered DNA curtain assays. We present cryo-EM structures of an ATAD2 family ATPase to atomic resolution in three different nucleotide states, revealing unique structural features required for histone loading on DNA, and directly visualize the transitions of Abo1 from an asymmetric spiral (ATP-state) to a symmetric ring (ADP- and apo-states) using high-speed atomic force microscopy (HS-AFM). Furthermore, we find that the acidic pore of ATP-Abo1 binds a peptide substrate which is suggestive of a histone tail. Based on these results, we propose a model whereby Abo1 facilitates H3–H4 loading by utilizing ATP.

Subject Areas: Biology and Bio-materials

Diamond Offline Facilities: Electron Bio-Imaging Centre (eBIC)
Instruments: Krios I-Titan Krios I at Diamond

Other Facilities: SciLifeLabs (Sweden); KBSI (South Korea)

Added On: 24/12/2019 02:32

Documents:
s41467-019-13743-9.pdf

Discipline Tags:

Genetics Structural biology Life Sciences & Biotech

Technical Tags:

Microscopy Electron Microscopy (EM) Cryo Electron Microscopy (Cryo EM)