体外观察组蛋白六聚体与芽殖酵母 Mcm2(复制螺旋酶的一个亚基)氨基末端区域的结合和解离。

IF 1.4 4区 生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY
Kohji Hizume
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引用次数: 0

摘要

在 DNA 复制过程中,模板链上形成核小体的核心组蛋白会被逐出,并与新合成的链结合,重新形成核小体。Mcm2是Mcm2-7复合物的一个亚基,而Mcm2-7复合物是复制螺旋酶的核心成分,它与组蛋白的氨基末端区域(Mcm2N)相互作用,并参与母体组蛋白向滞后链的再循环。本文对Mcm2N与组蛋白的相互作用进行了生化分析,以揭示Mcm2N回收组蛋白的分子机制。加入 Mcm2N 后,由 H3-H4 四聚体和 H2A-H2B 二聚体组成的组蛋白六聚体从组蛋白八聚体中分离出来,与 Mcm2N 形成复合物。在组蛋白伴侣 Nap1 的存在下,组蛋白六聚体(而非 H3-H4 四聚体)从 Mcm2N 中释放出来。另一种组蛋白伴侣蛋白FACT稳定了Mcm2N-组蛋白六聚体复合物,以防止Nap1依赖性解离。这项研究表明,组蛋白转移是通过Mcm2N和组蛋白伴侣进行的。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
In vitro observation of histone-hexamer association with and dissociation from the amino-terminal region of budding yeast Mcm2, a subunit of the replicative helicase.

During DNA replication, core histones that form nucleosomes on template strands are evicted and associate with newly synthesized strands to reform nucleosomes. Mcm2, a subunit of the Mcm2-7 complex, which is a core component of the replicative helicase, interacts with histones in the amino-terminal region (Mcm2N) and is involved in the parental histone recycling to lagging strands. Herein, the interaction of Mcm2N with histones was biochemically analyzed to reveal the molecular mechanisms underlying histone recycling by Mcm2N. With the addition of Mcm2N, a histone hexamer, comprising an H3-H4 tetramer and an H2A-H2B dimer, was excised from the histone octamer to form a complex with Mcm2N. The histone hexamer, but not H3-H4 tetramer was released from Mcm2N in the presence of Nap1, a histone chaperone. FACT, another histone chaperone, stabilized Mcm2N-histone hexamer complex to protect from Nap1-dependent dissociation. This study indicates cooperative histone transfer via Mcm2N and histone chaperones.

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来源期刊
Bioscience, Biotechnology, and Biochemistry
Bioscience, Biotechnology, and Biochemistry 生物-生化与分子生物学
CiteScore
3.50
自引率
0.00%
发文量
183
审稿时长
1 months
期刊介绍: Bioscience, Biotechnology, and Biochemistry publishes high-quality papers providing chemical and biological analyses of vital phenomena exhibited by animals, plants, and microorganisms, the chemical structures and functions of their products, and related matters. The Journal plays a major role in communicating to a global audience outstanding basic and applied research in all fields subsumed by the Japan Society for Bioscience, Biotechnology, and Agrochemistry (JSBBA).
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