RECA PROTEIN MEDIATES HOMOLOGOUS RECOGNITION VIA NON-WATSON-CRICK BONDS IN BASE TRIPLETS
RECA PROTEIN MEDIATES HOMOLOGOUS RECOGNITION VIA NON-WATSON-CRICK BONDS IN BASE TRIPLETS
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DOI：
10.1098/rstb.1995.0002
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发表时间：
1995-01-30
影响因子：
6.3
通讯作者：
RADDING, CM
中科院分区：
文献类型：
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作者：
RAO, BJ;RADDING, CM
大肠杆菌RecA蛋白是一类蛋白的原型，它在单链DNA上形成螺旋状核蛋白丝，识别双链DNA的同源性，并在同源重组中启动链交换。几年前这一反应的发现给人们带来了一个难题，即第三条链如何识别双链DNA的同源性。双链DNA的沃森-克里克键在一个由堆叠的碱基组成的疏水核心中面向内。最近的研究表明，RecA蛋白在碱基三联体中通过非沃森-克里克键促进同源识别。RecA反应中的中间体与非酶促形成的三联体DNA明显不同。RecA蛋白在重组中的重要性，以及同源蛋白在原核生物和真核生物中的广泛分布，表明了RecA蛋白影响同源识别的新型DNA相互作用的生物学意义。
E. coli RecA protein, the prototype of a class, forms a helical nucleoprotein filament on single-stranded DNA that recognizes homology in duplex DNA, and initiates the exchange of strands in homologous recombination. The discovery of this reaction some years ago posed a quandary on how a third strand recognizes homology in duplex DNA, whose Watson-Crick bonds face inward in a hydrophobic core of stacked bases. Recent studies have shown that RecA protein promotes homologous recognition via non-Watson-Crick bonds in base triplets. The intermediates in the RecA reaction differ distinctly from triplex DNA that forms non-enzymically. The biological significance of the novel set of DNA interactions by which RecA protein effects homologous recognition is indicated by the importance of this protein in recombination, and the widespread distribution of homologous proteins in prokaryotes and eukaryotes.