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Instruments / Technical Area	Publication Details	Published	Actions
Krios I-Titan Krios I at Diamond	Structural basis of nucleosome assembly by the Abo1 AAA+ ATPase histone chaperone Carol Cho , Juwon Jang , Yujin Kang , Hiroki Watanabe , Takayuki Uchihashi , Seung Joong Kim , Koichi Kato , Ja Yil Lee , Ji-Joon Song Nature Communications 10 DOI: 10.1038/s41467-019-13743-9 Diamond Proposal Number(s): [22985] Open Access Show Abstract ▼ 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.	Dec 2019

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Krios I-Titan Krios I at Diamond

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

Carol Cho , Juwon Jang , Yujin Kang , Hiroki Watanabe , Takayuki Uchihashi , Seung Joong Kim , Koichi Kato , Ja Yil Lee , Ji-Joon Song

Nature Communications 10

DOI: 10.1038/s41467-019-13743-9

Diamond Proposal Number(s): [22985]