Chromatin inheritance during cell division involves the replication of DNA and assembly of nucleosomes onto the replicated DNA, because passage of the DNA replication fork disrupts nucleosomes on the DNA. Half of the histones for the replication-coupled nucleosome assembly comes from the disrupted parental nucleosomes, and the other half is newly synthesized.
Chromatin assembly factor-1 is an evolutionarily conserved heterotrimeric protein complex that is responsible for the deposition of newly synthesized histones H3 and H4 onto DNA. However, the lack of structural information about CAF-1 has hindered the understanding of the molecular mechanism underlying de novo nucleosome assembly.on August 25, a research team led by Prof. Xu Ruiming from the Institute of Biophysics of the Chinese Academy of Sciences, in collaboration with Prof. Li Guohong, Prof.
The researchers first determined the crystal structure of the core domain of human CAF-1 in the absence of histones and theThe results showed that a CAF-1 complex binds to an H3-H4 heterodimer mainly through the p60 subunit and the ED loop of the p150 subunit.
The researchers also found that a 30-bp DNA oligomer triggers the dimerization of the CAF-1-H3-H4 complex, and solved the cryo-EM structure of a 2:2 CAF-1-H3-H4 complex.
Using a 147-bp DNA fragment, the researchers observed a CAF-1-bound right-handed di-tetrasome structure, which was further confirmed by the analysis using the single-molecule freely orbiting magnetic tweezer method at a physiological salt concentration.
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