期刊
MOLECULAR CELL
卷 71, 期 2, 页码 284-+出版社
CELL PRESS
DOI: 10.1016/j.molcel.2018.06.020
关键词
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资金
- Ministry of Science and Technology of China [2017YFA0504200, 2015CB856200]
- National Natural Science Foundation of China [31630041, 31525013, 31521002, 61275192, 11474346, 31471218]
- Chinese Academy of Sciences (CAS) Strategic Priority Research Program [XDB19040202]
- Key Research Program of Frontier Sciences, CAS [QYZDB-SSW-SLH045]
- Youth Innovation Promotion Association CAS [2015071]
- National Key Research and Development Program [2016YFA0301500]
- Key Research Program on Frontier Science [QYZDY-SSW-SMC020]
- HHMI international research scholar grant [55008737]
The human FACT (facilitates chromatin transcription) complex, composed of two subunits SPT16 (Suppressor of Ty 16) and SSRP1 (Structure-specific recognition protein-1), plays essential roles in nucleosome remodeling. However, the molecular mechanism of FACT reorganizing the nucleosome still remains elusive. In this study, we demonstrate that FACT displays dual functions in destabilizing the nucleosome and maintaining the original histones and nucleosome integrity at the single-nucleosome level. We found that the subunit SSRP1 is responsible for maintenance of nucleosome integrity by holding the H3/H4 tetramer on DNA and promoting the deposition of the H2A/H2B dimer onto the nucleosome. In contrast, the large subunit SPT16 destabilizes the nucleosome structure by displacing the H2A/H2B dimers. Our findings provide mechanistic insights by which the two subunits of FACT coordinate with each other to fulfill its functions and suggest that FACT may play essential roles in preserving the original histones with epigenetic identity during transcription or DNA replication.
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