Structural insights into histone binding and nucleosome assembly by chromatin assembly factor-1-Reference-Cited by-同舟云学术

Structural insights into histone binding and nucleosome assembly by chromatin assembly factor-1

Published:2023-08-25 Issue:6660 Volume:381 Page:
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Liu Chao-Pei¹^ORCID,Yu Zhenyu¹,Xiong Jun¹^ORCID,Hu Jie¹^ORCID,Song Aoqun¹^ORCID,Ding Dongbo¹^ORCID,Yu Cong¹²,Yang Na³^ORCID,Wang Mingzhu⁴^ORCID,Yu Juan¹^ORCID,Hou Peini¹^ORCID,Zeng Kangning¹⁵,Li Zhenyu⁶,Zhang Zhuqiang¹^ORCID,Zhang Xinzheng¹⁵^ORCID,Li Wei¹⁵^ORCID,Zhang Zhiguo⁷^ORCID,Zhu Bing¹⁵⁸^ORCID,Li Guohong¹⁵^ORCID,Xu Rui-Ming¹²⁵^ORCID

Affiliation:

1. National Laboratory of Biomacromolecules and Key Laboratory of Epigenetic Regulation and Intervention, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.

2. Key Laboratory of Systems Health Science of Zhejiang Province, School of Life Science, Hangzhou Institute for Advanced Study, University of Chinese Academy of Sciences, Hangzhou, Zhejiang 310024, China.

3. State Key Laboratory of Medicinal Chemical Biology, College of Pharmacy and Key Laboratory of Medical Data Analysis and Statistical Research of Tianjin, Nankai University, Tianjin 300353, China.

4. Institutes of Physical Science and Information Technology, Anhui University, Hefei, Anhui 230601, China.

5. School of Life Sciences, University of Chinese Academy of Sciences, Beijing 100049, China.

6. School of Physical Sciences, University of Chinese Academy of Sciences, Beijing 100049, China.

7. Institute for Cancer Genetics, Department of Pediatrics and Department of Genetics and Development, Columbia University Irving Medical Center, New York, NY 10032, USA.

8. New Cornerstone Science Laboratory, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Link

https://www.science.org/doi/pdf/10.1126/science.add8673

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