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(Received for publication, April 24, 1996, and in revised form, July 9, 1996)
From the Department of Pharmacology, University of Minnesota
Medical School, Minneapolis, Minnesota 55455
Mitochondrial protein extracts from normal and
immortalized mammalian somatic cells catalyze homologous recombination
of plasmid DNA substrates. Mitochondrial homologous recombination
activity required exogenous adenosine triphosphate, although
substantial activity remained when non-hydrolyzable analogs were used
instead. There was no requirement for added nucleoside triphosphates,
and the reaction was not inhibited by dideoxyadenosine triphosphate or
aphidicolin. The majority of recombinant plasmid molecules
result from a conservative process, indicating that
nuclease-mediated strand-annealing is not responsible for the
mitochondrial homologous recombination activity. Affinity-purified
anti-recA antibodies inhibited the reaction, suggesting
that activity is dependent on a mammalian mitochondrial homolog of the
bacterial strand-transferase protein. The presence of homologous
recombination activity within mammalian mitochondrial extracts suggests
that this process is involved in mitochondrial DNA repair.
Volume 271, Number 44,
Issue of November 1, 1996
pp. 27536-27543
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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