scholarly journals The direction of RecA protein assembly onto single strand DNA is the same as the direction of strand assimilation during strand exchange.

1985 ◽  
Vol 260 (22) ◽  
pp. 12308-12312 ◽  
Author(s):  
J C Register ◽  
J Griffith
Biochimie ◽  
1991 ◽  
Vol 73 (4) ◽  
pp. 515-517 ◽  
Author(s):  
Zˇ. Trovcˇević ◽  
M. Petranović ◽  
K. Brcˇić-Kostić ◽  
D. Petranović ◽  
N. Lersˇ ◽  
...  

1987 ◽  
Vol 7 (9) ◽  
pp. 3124-3130 ◽  
Author(s):  
D Ganea ◽  
P Moore ◽  
L Chekuri ◽  
R Kucherlapati

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.


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