EMD-33631
Cryo-EM structure of the two CAF1LCs bound right-handed Di-tetrasome
EMD-33631
Single-particle5.6 Å
Deposition: 18/06/2022Map released: 16/08/2023
Last modified: 06/09/2023
Sample Organism:
Homo sapiens,
synthetic construct
Sample: Two CAF1LCs bound right-handed Di-tetrasome
Fitted models: 7y61 (Avg. Q-score: 0.189)
Deposition Authors: Liu CP
,
Yu ZY,
Yu C,
Xu RM
Sample: Two CAF1LCs bound right-handed Di-tetrasome
Fitted models: 7y61 (Avg. Q-score: 0.189)
Deposition Authors: Liu CP
,
Yu ZY,
Yu C,
Xu RM
Structural insights into histone binding and nucleosome assembly by chromatin assembly factor-1.
Liu CP ,
Yu Z,
Xiong J ,
Hu J ,
Song A ,
Ding D ,
Yu C,
Yang N ,
Wang M ,
Yu J ,
Hou P ,
Zeng K,
Li Z,
Zhang Z ,
Zhang X ,
Li W ,
Zhang Z ,
Zhu B ,
Li G ,
Xu RM
(2023) Science , 381 , eadd8673 - eadd8673
,
Yu Z,
Xiong J ,
Hu J ,
Song A ,
Ding D ,
Yu C,
Yang N ,
Wang M ,
Yu J ,
Hou P ,
Zeng K,
Li Z,
Zhang Z ,
Zhang X ,
Li W ,
Zhang Z ,
Zhu B ,
Li G ,
Xu RM
(2023) Science , 381 , eadd8673 - eadd8673
Abstract:
Chromatin inheritance entails de novo nucleosome assembly after DNA replication by chromatin assembly factor-1 (CAF-1). Yet direct knowledge about CAF-1's histone binding mode and nucleosome assembly process is lacking. In this work, we report the crystal structure of human CAF-1 in the absence of histones and the cryo-electron microscopy structure of CAF-1 in complex with histones H3 and H4. One histone H3-H4 heterodimer is bound by one CAF-1 complex mainly through the p60 subunit and the acidic domain of the p150 subunit. We also observed a dimeric CAF-1-H3-H4 supercomplex in which two H3-H4 heterodimers are poised for tetramer assembly and discovered that CAF-1 facilitates right-handed DNA wrapping of H3-H4 tetramers. These findings signify the involvement of DNA in H3-H4 tetramer formation and suggest a right-handed nucleosome precursor in chromatin replication.
Chromatin inheritance entails de novo nucleosome assembly after DNA replication by chromatin assembly factor-1 (CAF-1). Yet direct knowledge about CAF-1's histone binding mode and nucleosome assembly process is lacking. In this work, we report the crystal structure of human CAF-1 in the absence of histones and the cryo-electron microscopy structure of CAF-1 in complex with histones H3 and H4. One histone H3-H4 heterodimer is bound by one CAF-1 complex mainly through the p60 subunit and the acidic domain of the p150 subunit. We also observed a dimeric CAF-1-H3-H4 supercomplex in which two H3-H4 heterodimers are poised for tetramer assembly and discovered that CAF-1 facilitates right-handed DNA wrapping of H3-H4 tetramers. These findings signify the involvement of DNA in H3-H4 tetramer formation and suggest a right-handed nucleosome precursor in chromatin replication.