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一个包含 Est1 募集蛋白的酵母端粒酶复合物在细胞周期的早期组装。

A yeast telomerase complex containing the Est1 recruitment protein is assembled early in the cell cycle.

机构信息

Salk Institute for Biological Studies, La Jolla, CA 92037, USA.

出版信息

Biochemistry. 2013 Feb 19;52(7):1131-3. doi: 10.1021/bi3015218. Epub 2013 Feb 7.

DOI:10.1021/bi3015218
PMID:23390975
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4172482/
Abstract

In budding yeast, association of the Est1 regulatory protein with telomerase is thought to be limited to the late S phase, when telomere elongation occurs. By monitoring the stoichiometry of telomerase subunits, we show instead that a telomerase complex containing Est1 is assembled much earlier in the cell cycle. We also report a biochemical interaction between Est1 and the telomere binding protein Cdc13 that recapitulates the previously observed genetic relationship between EST1 and CDC13. This supports a model in which regulated binding of Cdc13 to chromosome termini dictates subsequent interaction of a recruitment-competent telomerase complex with telomeres.

摘要

在芽殖酵母中,Est1 调节蛋白与端粒酶的结合被认为仅限于晚期 S 期,此时发生端粒延伸。通过监测端粒酶亚基的化学计量,我们反而表明,含有 Est1 的端粒酶复合物在细胞周期的早期就已组装。我们还报告了 Est1 和端粒结合蛋白 Cdc13 之间的生化相互作用,这再现了 EST1 和 CDC13 之间先前观察到的遗传关系。这支持了这样一种模型,即 Cdc13 与染色体末端的调节结合决定了随后具有招募能力的端粒酶复合物与端粒的相互作用。

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本文引用的文献

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Live cell imaging of telomerase RNA dynamics reveals cell cycle-dependent clustering of telomerase at elongating telomeres.端粒酶 RNA 动力学的活细胞成像显示端粒酶在伸长的端粒处呈现细胞周期依赖性聚集。
Mol Cell. 2011 Dec 9;44(5):819-27. doi: 10.1016/j.molcel.2011.09.020.
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The telomeric Cdc13 protein interacts directly with the telomerase subunit Est1 to bring it to telomeric DNA ends in vitro.
从汉逊德巴利酵母端粒酶看 Est3 的结构与功能。
Sci Rep. 2020 Jul 6;10(1):11109. doi: 10.1038/s41598-020-68107-x.
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The mechanisms of K. lactis Cdc13 in telomere DNA-binding and telomerase regulation.酿酒酵母 Cdc13 在端粒 DNA 结合和端粒酶调控中的作用机制。
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Using Separation-of-Function Mutagenesis To Define the Full Spectrum of Activities Performed by the Est1 Telomerase Subunit .利用功能分离突变来定义 Est1 端粒酶亚基所执行的全部活动。
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