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

Cited 7 time in webofscience Cited 0 time in scopus
  • Hit : 231
  • Download : 59
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.
Publisher
NATURE PUBLISHING GROUP
Issue Date
2019-12
Language
English
Article Type
Article
Citation

NATURE COMMUNICATIONS, v.10, pp.5764 - 13page

ISSN
2041-1723
DOI
10.1038/s41467-019-13743-9
URI
http://hdl.handle.net/10203/270932
Appears in Collection
PH-Journal Papers(저널논문)BS-Journal Papers(저널논문)
Files in This Item
Cho_NatureCom2019.pdf(5.38 MB)Download
This item is cited by other documents in WoS
⊙ Detail Information in WoSⓡ Click to see webofscience_button
⊙ Cited 7 items in WoS Click to see citing articles in records_button

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0