BROWSE

Related Researcher

Author's Photo

Lee, Ja Yil
School of Life Sciences
Research Interests
  • Investigated eukaryotic homologous recombination.

ITEM VIEW & DOWNLOAD

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

Cited 0 times inthomson ciCited 0 times inthomson ci
Title
Structural basis of nucleosome assembly by the Abo1 AAA+ ATPase histone chaperone
Author
Cho, CarolJang, JuwonKang, YujinWatanabe, HirokiUchihashi, TakayukiKim, Seung JoongKato, KoichiLee, Ja YilSong, Ji-Joon
Issue Date
2019-12
Publisher
Nature Publishing Group
Citation
NATURE COMMUNICATIONS, v.10, pp.5764
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.
URI
https://scholarworks.unist.ac.kr/handle/201301/30660
URL
https://www.nature.com/articles/s41467-019-13743-9
DOI
10.1038/s41467-019-13743-9
ISSN
2041-1723
Appears in Collections:
SLS_Journal Papers
Files in This Item:
s41467-019-13743-9.pdf Download

find_unist can give you direct access to the published full text of this article. (UNISTARs only)

Show full item record

qrcode

  • mendeley

    citeulike

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

MENU