Chz1, a nuclear chaperone for histone H2AZ

Chz1, a nuclear chaperone for histone H2AZ
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DOI:
10.1016/j.molcel.2006.12.015
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发表时间:
2007-02-09
期刊:
影响因子:
16
通讯作者:
Wu, Carl
Wu, Carl
中科院分区:
生物学1区
文献类型:
--
作者:
Luk, Ed;Vu, Ngoc-Diep;Wu, Carl

文献摘要

被引文献

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组蛋白变体 H2AZ 标记了芽殖酵母大多数基因启动子侧翼的核小体。 H2AZ 掺入染色质依赖于 SWR1 复合物,该复合物催化 H2AZ 取代传统组蛋白 H2A。在细胞中,未掺入的组蛋白 H2AZ 池先前已被发现与 Nap1(传统组蛋白 H2A-H2B 的伴侣)相关。在这里,我们报告了 Chz1 的发现,它是一种组蛋白伴侣,对 H2AZ 有偏好,并且还可以为 SWR1 依赖性组蛋白替换提供组蛋白变体的来源。细菌表达的 Chz1 与 H2AZ-H2B 形成异源三聚体,稳定组蛋白二聚体的结合。我们在 Chz1 的 H2AZ 相互作用域内发现了一个对于组蛋白变体识别很重要的保守基序。该基序在其他后生动物蛋白中的存在表明 H2AZ 特异性伴侣可能是广泛保守的。
The histone variant H2AZ marks nucleosomes flanking the promoters of most genes of budding yeast. The incorporation of H2AZ into chromatin is dependent on the SWR1 complex, which catalyses the replacement of conventional histone H2A with H2AZ. In cells, the pool of unincorporated histone H2AZ has previously been found in association with Nap1, a chaperone for conventional histone H2A-H2B. Here, we report the discovery of Chz1, a histone chaperone that has preference for H2AZ and can also deliver a source of the histone variant for SWR1-dependent histone replacement. Bacterially expressed Chz1 forms a heterotrimer with H2AZ-H2B, stabilizing the association of the histone dimer. We have identified a conserved motif important for histone variant recognition within the H2AZ-interacting domain of Chz1. The presence of this motif in other metazoan proteins suggests that H2AZ-specific chaperones may be widely conserved.