由RecA家族重组蛋白促进的DNA链交换的极性。
Polarity of DNA strand exchange promoted by recombination proteins of the RecA family.
作者信息
Gupta R C, Golub E I, Wold M S, Radding C M
机构信息
Department of Genetics, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06510, USA.
出版信息
Proc Natl Acad Sci U S A. 1998 Aug 18;95(17):9843-8. doi: 10.1073/pnas.95.17.9843.
Abstract
Homologs of Escherichia coli RecA recombination protein, which have been found throughout the living kingdom, promote homologous pairing and strand exchange. The nucleoprotein filament, within which strand exchange occurs, has been conserved through evolution, but conservation of the polarity of exchange and the significance of that directionality has not been settled. Using oligonucleotides as substrates, and assays based on fluorescence resonance energy transfer (FRET), we distinguished the biased formation of homologous joints at either end of duplex DNA from the subsequent directionality of strand exchange. As with E. coli RecA protein, the homologous Rad51 proteins from both Homo sapiens (HsRad51) and Saccharomyces cerevisiae (ScRad51) propagated DNA strand exchange preferentially in the 5' to 3' direction. The data suggest that 5' to 3' polarity is a conserved intrinsic property of recombination filaments.
摘要
在整个生物界都已发现的大肠杆菌RecA重组蛋白的同源物，能够促进同源配对和链交换。发生链交换的核蛋白丝在进化过程中得以保留，但交换极性的保守性以及该方向性的意义尚未确定。我们使用寡核苷酸作为底物，并基于荧光共振能量转移（FRET）进行检测，区分了双链DNA两端同源接头的偏向形成与随后的链交换方向性。与大肠杆菌RecA蛋白一样，来自智人（HsRad51）和酿酒酵母（ScRad51）的同源Rad51蛋白优先在5'至3'方向上进行DNA链交换。数据表明，5'至3'极性是重组丝保守的内在特性。
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本文引用的文献
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