Destruction of quadruplex by proteins, and its biological implications in replication and telomere maintenance.

Nucleic acids research. Supplement (2001) Pub Date : 2003-01-01 DOI:10.1093/nass/3.1.231

Yoshiaki Enokizono, Akimasa Matsugami, Seiichi Uesugi, Hirokazu Fukuda, Naoto Tsuchiya, Takashi Sugimura, Minako Nagao, Hitoshi Nakagama, Masato Katahira

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引用次数: 6

Abstract

The minisatellite DNA Pc-1 consists of tandem repeats of d(GGCAG). We previously reported that a d(GGCAG)n strand folds into an intramolecular quadruplex under physiological conditions and that during replication the progression of DNA polymerase is blocked by the quadruplex in vitro. Therefore, the formation of the quadruplex was supposed to be responsible for the hypermutable features of Pc-1. Then, we have identified proteins that bind to Pc-1, one of which is hnRNP A1. Here, we have demonstrated that hnRNP A1 destroys the quadruplex of Pc-1 on binding and abrogates the arrest of DNA polymerase at the repeat. Thus, hnRNP A1 functions as if it is a chaperon to assist Pc-1 DNA to form the proper folding suitable for replication. We have also found that hnRNP A1 and a related protein, hnRNP D, destroy the quadruplex of telomere DNA, which suggests the involvement of these proteins in telomere maintenance as DNA chaperons.

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蛋白质对四重体的破坏及其在复制和端粒维持中的生物学意义。

微卫星DNA Pc-1由d(GGCAG)串联重复序列组成。我们之前报道了d(GGCAG)n链在生理条件下折叠成分子内四重体，并且在体外复制过程中DNA聚合酶的进展被四重体阻断。因此，四重结构的形成被认为是Pc-1的超可变特性的原因。然后，我们已经确定了与Pc-1结合的蛋白质，其中一个是hnRNP A1。在这里，我们已经证明了hnRNP A1在结合Pc-1时破坏了四重体，并在重复中取消了DNA聚合酶的捕获。因此，hnRNP A1的功能就像是一个伴侣，帮助Pc-1 DNA形成适合复制的适当折叠。我们还发现hnRNP A1和相关蛋白hnRNP D破坏端粒DNA的四重体，这表明这些蛋白作为DNA伴侣参与端粒维持。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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Nucleic acids research. Supplement (2001)

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