Japan Agency for Medical Research and Development (AMED)
JP17am0101073
Japan
Japan Agency for Medical Research and Development (AMED)
JP17am0101072j0001
Japan
Japan Society for the Promotion of Science
JP26251008
Japan
Japan Society for the Promotion of Science
JP16K18528
Japan
Japan Society for the Promotion of Science
JP16H01410
Japan
Japan Society for the Promotion of Science
JP17K07313
Japan
Japan Society for the Promotion of Science
18K06089
Japan
Japan Society for the Promotion of Science
JP18K06064
Japan
Japan Society for the Promotion of Science
JP26505009
Japan
Japan Agency for Medical Research and Development (AMED)
JP17am0101076
Japan
Japan Science and Technology
JPMJPR12L9
Japan
Citation
Journal: Sci Rep / Year: 2019 Title: Structural visualization of key steps in nucleosome reorganization by human FACT. Authors: Kouta Mayanagi / Kazumi Saikusa / Naoyuki Miyazaki / Satoko Akashi / Kenji Iwasaki / Yoshifumi Nishimura / Kosuke Morikawa / Yasuo Tsunaka / Abstract: Facilitates chromatin transcription (FACT) is a histone chaperone, which accomplishes both nucleosome assembly and disassembly. Our combined cryo-electron microscopy (EM) and native mass spectrometry ...Facilitates chromatin transcription (FACT) is a histone chaperone, which accomplishes both nucleosome assembly and disassembly. Our combined cryo-electron microscopy (EM) and native mass spectrometry (MS) studies revealed novel key steps of nucleosome reorganization conducted by a Mid domain and its adjacent acidic AID segment of human FACT. We determined three cryo-EM structures of respective octasomes complexed with the Mid-AID and AID regions, and a hexasome alone. We discovered extensive contacts between a FACT region and histones H2A, H2B, and H3, suggesting that FACT is competent to direct functional replacement of a nucleosomal DNA end by its phosphorylated AID segment (pAID). Mutational assays revealed that the aromatic and phosphorylated residues within pAID are essential for octasome binding. The EM structure of the hexasome, generated by the addition of Mid-pAID or pAID, indicated that the dissociation of H2A-H2B dimer causes significant alteration from the canonical path of the nucleosomal DNA.
#1: Journal: Genes Dev / Year: 2016 Title: Integrated molecular mechanism directing nucleosome reorganization by human FACT. Authors: Yasuo Tsunaka / Yoshie Fujiwara / Takuji Oyama / Susumu Hirose / Kosuke Morikawa / Abstract: Facilitates chromatin transcription (FACT) plays essential roles in chromatin remodeling during DNA transcription, replication, and repair. Our structural and biochemical studies of human FACT- ...Facilitates chromatin transcription (FACT) plays essential roles in chromatin remodeling during DNA transcription, replication, and repair. Our structural and biochemical studies of human FACT-histone interactions present precise views of nucleosome reorganization, conducted by the FACT-SPT16 (suppressor of Ty 16) Mid domain and its adjacent acidic AID segment. AID accesses the H2B N-terminal basic region exposed by partial unwrapping of the nucleosomal DNA, thereby triggering the invasion of FACT into the nucleosome. The crystal structure of the Mid domain complexed with an H3-H4 tetramer exhibits two separate contact sites; the Mid domain forms a novel intermolecular β structure with H4. At the other site, the Mid-H2A steric collision on the H2A-docking surface of the H3-H4 tetramer within the nucleosome induces H2A-H2B displacement. This integrated mechanism results in disrupting the H3 αN helix, which is essential for retaining the nucleosomal DNA ends, and hence facilitates DNA stripping from histone.
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