Keener S L, McEntee K
Nucleic Acids Res. 1984 Aug 10;12(15):6127-39. doi: 10.1093/nar/12.15.6127.
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 noncomplementary regions.
RecA蛋白催化含有互补序列的环状单链DNA分子对之间的退火反应，互补序列的长度从3550个核苷酸到181个核苷酸不等。该反应需要ATP和催化量的recA蛋白。含有大的互补插入片段的分子被recA蛋白退火形成大的多聚体聚集体，这些聚集体在琼脂糖凝胶中迁移缓慢。相比之下，由含有短互补区域的环状分子形成的产物主要是二聚体结构。我们利用电子显微镜、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，在没有自由末端且这些序列两侧有大量非互补区域的情况下，recA蛋白催化互补DNA序列之间的多个成核事件。
