真核生物同源重组的生物化学。

Wolf-Dietrich Heyer
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引用次数: 74

摘要

随着Rad51蛋白是细菌RecA蛋白和T4 UvsX蛋白的真核同源物的发现,真核同源重组的生物化学研究开始火热起来;这个领域仍然很热门。同源重组、同源搜索和DNA链入侵等核心反应,以及催化该反应的蛋白质,原则上在整个进化过程中是保守的。然而,真核生物基因组复杂性的增加和真核细胞生物学的多样性给重组机制带来了额外的挑战。这种复杂性的增加与新的重组蛋白和新的支持途径的进化,以及那些在进化中明显保守的真核重组蛋白性质的变化相一致,这并不奇怪。在人类中,同源重组中的缺陷导致癌症易感性增加,强调了该途径对基因组稳定性和肿瘤抑制的重要性。本文将通过对酵母和人蛋白的生化分析,对真核生物中同源重组的机制进行综述。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Biochemistry of eukaryotic homologous recombination.

The biochemistry of eukaryotic homologous recombination caught fire with the discovery that Rad51 is the eukaryotic homolog of the bacterial RecA and T4 UvsX proteins; and this field is still hot. The core reaction of homologous recombination, homology search and DNA strand invasion, along with the proteins catalyzing it, are conserved throughout evolution in principle. However, the increased complexity of eukaryotic genomes and the diversity of eukaryotic cell biology pose additional challenges to the recombination machinery. It is not surprising that this increase in complexity coincided with the evolution of new recombination proteins and novel support pathways, as well as changes in the properties of those eukaryotic recombination proteins that are evidently conserved in evolution. In humans, defects in homologous recombination lead to increased cancer predisposition, underlining the importance of this pathway for genomic stability and tumor suppression. This review will focus on the mechanisms of homologous recombination in eukaryotes as elucidated by the biochemical analysis of yeast and human proteins.

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