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首页> 外文期刊>Nucleic acids research >Homologous pairing of single-stranded circular DNAs catalyzed by recA protein
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Homologous pairing of single-stranded circular DNAs catalyzed by recA protein

机译:通过RECA蛋白催化的单链圆形DNA的同源配对

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RecA protein catalyzes annealing between pairs of circular single-stranded DNA molecules containing complementary sequences varying in length from 3550 nucleotides to 181 nucleotides. The reaction requires ATP and catalytic amounts of recA protein. Molecules containing large complementary inserts are annealed by recA protein to form large multimeric aggregates that migrate slowly in agarose gels. In contrast the products formed from circular molecules containing short complementary regions are principally dimeric structures. We have used electron microscopy, thermal denaturation and kinetic studies to analyze these reaction products. Our results indicate that recA protein catalyzes multiple nucleation events between complementary DNA sequences in the absence of a free end and when these sequences are flanked by extensive noncomplemnentary regions.
机译:RECA蛋白质催化在含有长度的循环单链DNA分子与长度为3550个核苷酸至181个核苷酸的循环单链DNA分子之间的退火。反应需要ATP和催化量的RECA蛋白。含有大互补插入物的分子由RECA蛋白退火,形成大的多聚体聚集体,其在琼脂糖凝胶中缓慢迁移。相反,由含有短互补区域的圆形分子形成的产物主要是二聚体结构。我们使用电子显微镜,热变性和动力学研究来分析这些反应产物。我们的结果表明,在没有自由端的互补DNA序列之间催化重蛋白蛋白质在没有自由末端,并且当这些序列侧翼被广泛的非责备区域侧翼时。

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