Ganea D, Moore P, Chekuri L, Kucherlapati R
Center for Genetics, University of Illinois College of Medicine, Chicago 60612.
Mol Cell Biol. 1987 Sep;7(9):3124-30. doi: 10.1128/mcb.7.9.3124-3130.1987.
We have characterized an enzymatic activity from human cell nuclei which is capable of catalyzing strand exchange between homologous DNA sequences. The strand exchange activity was Mg2+ dependent and required ATP hydrolysis. In addition, it was capable of promoting reannealing of homologous DNA sequences and could form nucleoprotein networks in a fashion reminiscent of purified bacterial RecA protein. Using an in vitro recombination assay, we also showed that the strand exchange activity was biologically important. The factor(s) responsible for the activity has been partially purified.
我们已经鉴定了一种来自人类细胞核的酶活性，它能够催化同源DNA序列之间的链交换。链交换活性依赖于Mg2+，并且需要ATP水解。此外，它能够促进同源DNA序列的重新退火，并且能够以类似于纯化的细菌RecA蛋白的方式形成核蛋白网络。使用体外重组试验，我们还表明链交换活性在生物学上是重要的。负责该活性的因子已被部分纯化。
