Open AccessThe Histone Chaperone FACT Contributes to DNA Replication-Coupled Nucleosome Assembly
Author(s) -
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
Publication year - 2016
Publication title -
cell reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.264
H-Index - 154
eISSN - 2639-1856
pISSN - 2211-1247
DOI - 10.1016/j.celrep.2015.12.096
Subject(s) - nucleosome , histone code , microbiology and biotechnology , histone , histone h1 , histone octamer , histone methylation , histone h2a , biology , histone methyltransferase , chaperone (clinical) , chromatin , genetics , chemistry , dna , dna methylation , gene , medicine , gene expression , pathology
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.
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