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RAP1蛋白在体内与酵母端粒相互作用:过量表达会改变端粒结构并降低染色体稳定性。

RAP1 protein interacts with yeast telomeres in vivo: overproduction alters telomere structure and decreases chromosome stability.

作者信息

Conrad M N, Wright J H, Wolf A J, Zakian V A

机构信息

Fred Hutchinson Cancer Research Center, Seattle, Washington 98104.

出版信息

Cell. 1990 Nov 16;63(4):739-50. doi: 10.1016/0092-8674(90)90140-a.

Abstract

The protein encoded by the RAP1 gene of S. cerevisiae binds in vitro to a consensus sequence occurring at a number of sites in the yeast genome, including the repeated sequence C2-3A(CA)1-6 found at yeast telomeres. We present two lines of evidence for the in vivo binding of RAP1 protein at telomeres: first, RAP1 is present in telomeric chromatin and second, alterations in the level of RAP1 protein affect telomere length. The length changes seen with under- and overexpression of RAP1 are consistent with the interpretation that RAP1 binding to telomeres protects them from degradation. Unexpectedly, overproduction of the RAP1 protein was also shown to decrease greatly chromosome stability, suggesting that RAP1 mediates interactions that have a more global effect on chromosome behavior than simply protecting telomeres from degradation. Such interactions may involve telomere associations both with other telomeres and/or with structural elements of the nucleus.

摘要

酿酒酵母RAP1基因编码的蛋白质在体外与酵母基因组中多个位点出现的共有序列结合,包括在酵母端粒处发现的重复序列C2 - 3A(CA)1 - 6。我们提供了两条关于RAP1蛋白在端粒处体内结合的证据:第一,RAP1存在于端粒染色质中;第二,RAP1蛋白水平的改变会影响端粒长度。RAP1表达不足和过量表达时观察到的长度变化与RAP1结合端粒可保护其免受降解的解释一致。出乎意料的是,RAP1蛋白的过量产生也被证明会大大降低染色体稳定性,这表明RAP1介导的相互作用对染色体行为具有比简单保护端粒免受降解更广泛的影响。这种相互作用可能涉及端粒与其他端粒和/或细胞核结构元件的关联。

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