Replication-independent histone deposition by the HIR complex and Asf1
Replication-independent histone deposition by the HIR complex and Asf1
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DOI:
10.1016/j.cub.2005.10.053
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发表时间:
2005-11-22
期刊:
影响因子:
9.2
通讯作者:
Kaufman, PD
中科院分区:
文献类型:
--
作者:
Green, EM;Antczak, AJ;Kaufman, PD
The orderly deposition of histones onto DNA is mediated by conserved assembly complexes, including chromatin assembly factor-1 (CAF-1) and the Hir proteins [1-4]. CAF-1 and the Hir proteins operate in distinct but functionally overlapping histone deposition pathways in vivo [5, 6]. The Hir proteins and CAF-1 share a common partner, the highly conserved histone H3/H4 binding protein Asf1, which binds the middle subunit of CAF-1 as well as to Hir proteins [7-11]. Asf1 binds to newly synthesized histones H3/H4 [12], and this complex stimulates histone deposition by CAF-1 [7,11,12]. In yeast, Asf1 is required for the contribution of the Hir proteins to gene silencing [7, 13]. Here, we demonstrate that HIM, Hir2, Hir3, and Hpc2 comprise the HIR complex, which copurifies with the histone deposition protein Asf1. Together, the HIR complex and Asf1 deposit histones onto DNA in a replication-independent manner. Histone deposition by the HIR complex and Asf1 is impaired by a mutation in Asf1 that inhibits HIR binding. These data indicate that the HIR complex and Asf1 proteins function together as a conserved eukaryotic pathway for histone replacement throughout the cell cycle.