Characterization of an ATP-dependent DNA strand transferase from human cells.
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.
Ganea
D
D
Center for Genetics, University of Illinois College of Medicine, Chicago 60612.
Moore
P
P
Chekuri
L
L
Kucherlapati
R
R
D000251:Adenosine Triphosphatases / Q000302:isolation & purification / Q000502:physiology*; D002467:Cell Nucleus / Q000201:enzymology; D004247:DNA / Q000378:metabolism*; D004254:DNA Nucleotidyltransferases; D003852:Deoxyribonucleoproteins / Q000378:metabolism; D006801:Humans; D009695:Nucleic Acid Renaturation; D009713:Nucleotidyltransferases / Q000302:isolation & purification / Q000502:physiology*; D011995:Recombination, Genetic; D012689:Sequence Homology, Nucleic Acid
D003852:Deoxyribonucleoproteins; D004247:DNA; C054059:ATP-dependent DNA strand transferase; D004254:DNA Nucleotidyltransferases; D009713:Nucleotidyltransferases; D000251:Adenosine Triphosphatases