Unusual stability of recombination intermediates made by Escherichia coli RecA protein.

摘要: The structure and stability of recombination intermediates made by RecA protein have been investigated following deproteinization. consist two duplex DNA molecules connected a junction, as visualized electron microscopy. Although we expected the structures to be highly unstable due branch migration this was not case. Instead, found that were stable at 37 degrees C. At 56 C, greater than 60% remained after 6 h incubation. Only higher temperatures significant observed. This unexpected suggests formation extensive lengths heteroduplex in Escherichia coli is likely require continued action proteins, does occur via spontaneous migration. We show may formed vitro ATP-dependent strand exchange catalysed or RuvA RuvB proteins E. coli.