The Histone Chaperone FACT Contributes to DNA Replication-Coupled Nucleosome Assembly
Summary: DNA replication-coupled (RC) nucleosome assembly is mediated by histone chaperones and is fundamental for epigenetic inheritance and maintenance of genomic integrity. The mechanisms that promote this process are only partially understood. Here, we show that the histone chaperone FACT (facil...
| Main Authors: | , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2016-02-01
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| Series: | Cell Reports |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124715015521 |
| _version_ | 1818034496616792064 |
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| author | Jiayi Yang Xu Zhang Jianxun Feng He Leng Shuqi Li Junyu Xiao Shaofeng Liu Zhiyun Xu Jiawei Xu Di Li Zhongshi Wang Jingyang Wang Qing Li |
| author_facet | Jiayi Yang Xu Zhang Jianxun Feng He Leng Shuqi Li Junyu Xiao Shaofeng Liu Zhiyun Xu Jiawei Xu Di Li Zhongshi Wang Jingyang Wang Qing Li |
| author_sort | Jiayi Yang |
| collection | DOAJ |
| description | Summary: DNA replication-coupled (RC) nucleosome assembly is mediated by histone chaperones and is fundamental for epigenetic inheritance and maintenance of genomic integrity. The mechanisms that promote this process are only partially understood. Here, we show that the histone chaperone FACT (facilitates chromatin transactions), consisting of Spt16 and Pob3, promotes newly synthesized histone H3-H4 deposition. We describe an allele of Spt16 (spt16-m) that has a defect in binding to H3-H4 and impairs their deposition onto DNA. Consistent with a direct role for FACT in RC nucleosome assembly, spt16-m displays synthetic defects with other histone chaperones associated with this process, CAF-1 and Rtt106. Importantly, we show that FACT physically associates with Rtt106 and that the acetylation of H3K56, a mark on newly synthesized H3, modulates this interaction. Therefore, FACT collaborates with CAF-1 and Rtt106 in RC nucleosome assembly. : Yang et al. show that mutation of Spt16, a FACT subunit, impairs the replication-coupled histone H3-H4 deposition. Mechanistically, FACT binds H3-H4 and cooperates with other histone chaperones, CAF-1 and Rtt106, to participate in replication-coupled nucleosome assembly. |
| first_indexed | 2024-12-10T06:40:05Z |
| format | Article |
| id | doaj.art-666bfb95403d4a9eba61d94219192cd8 |
| institution | Directory Open Access Journal |
| issn | 2211-1247 |
| language | English |
| last_indexed | 2024-12-10T06:40:05Z |
| publishDate | 2016-02-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Cell Reports |
| spelling | doaj.art-666bfb95403d4a9eba61d94219192cd82022-12-22T01:58:49ZengElsevierCell Reports2211-12472016-02-0114511281141The Histone Chaperone FACT Contributes to DNA Replication-Coupled Nucleosome AssemblyJiayi Yang0Xu Zhang1Jianxun Feng2He Leng3Shuqi Li4Junyu Xiao5Shaofeng Liu6Zhiyun Xu7Jiawei Xu8Di Li9Zhongshi Wang10Jingyang Wang11Qing Li12State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences and Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, ChinaState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences and Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, ChinaState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences and Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, ChinaState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences and Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, China; Academy for Advanced Interdisciplinary Studies, Peking University, Beijing 100871, ChinaState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences and Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, China; Academy for Advanced Interdisciplinary Studies, Peking University, Beijing 100871, ChinaState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences and Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, ChinaState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences and Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, China; School of Life Sciences, Tsinghua University, Beijing 100084, ChinaState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences and Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, ChinaState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences and Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, ChinaState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences and Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, ChinaState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences and Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, ChinaState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences and Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, ChinaState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences and Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, China; Corresponding authorSummary: DNA replication-coupled (RC) nucleosome assembly is mediated by histone chaperones and is fundamental for epigenetic inheritance and maintenance of genomic integrity. The mechanisms that promote this process are only partially understood. Here, we show that the histone chaperone FACT (facilitates chromatin transactions), consisting of Spt16 and Pob3, promotes newly synthesized histone H3-H4 deposition. We describe an allele of Spt16 (spt16-m) that has a defect in binding to H3-H4 and impairs their deposition onto DNA. Consistent with a direct role for FACT in RC nucleosome assembly, spt16-m displays synthetic defects with other histone chaperones associated with this process, CAF-1 and Rtt106. Importantly, we show that FACT physically associates with Rtt106 and that the acetylation of H3K56, a mark on newly synthesized H3, modulates this interaction. Therefore, FACT collaborates with CAF-1 and Rtt106 in RC nucleosome assembly. : Yang et al. show that mutation of Spt16, a FACT subunit, impairs the replication-coupled histone H3-H4 deposition. Mechanistically, FACT binds H3-H4 and cooperates with other histone chaperones, CAF-1 and Rtt106, to participate in replication-coupled nucleosome assembly.http://www.sciencedirect.com/science/article/pii/S2211124715015521 |
| spellingShingle | Jiayi Yang Xu Zhang Jianxun Feng He Leng Shuqi Li Junyu Xiao Shaofeng Liu Zhiyun Xu Jiawei Xu Di Li Zhongshi Wang Jingyang Wang Qing Li The Histone Chaperone FACT Contributes to DNA Replication-Coupled Nucleosome Assembly Cell Reports |
| title | The Histone Chaperone FACT Contributes to DNA Replication-Coupled Nucleosome Assembly |
| title_full | The Histone Chaperone FACT Contributes to DNA Replication-Coupled Nucleosome Assembly |
| title_fullStr | The Histone Chaperone FACT Contributes to DNA Replication-Coupled Nucleosome Assembly |
| title_full_unstemmed | The Histone Chaperone FACT Contributes to DNA Replication-Coupled Nucleosome Assembly |
| title_short | The Histone Chaperone FACT Contributes to DNA Replication-Coupled Nucleosome Assembly |
| title_sort | histone chaperone fact contributes to dna replication coupled nucleosome assembly |
| url | http://www.sciencedirect.com/science/article/pii/S2211124715015521 |
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