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JBC, Vol. 252, Issue 2, 499-503, Jan, 1977
D. C. Eichler and I. R. Lehman
The deoxyribonuclease specified by the recB and recC genes of Escherichia
coli (recBC DNase; exonuclease V) has been purified to near homogeneity by
a new procedure. Although hydrolysis of even a single nucleotide from a
duplex DNA molecule by the pure enzyme is absolutely dependent upon ATP,
the extent of phosphodiester hydrolysis is strongly inhibited by ATP
concentrations of 0.2 mm or greater, and the initial rate is unaffected.
Under these conditions, the extent of DNA hydrolysis is proportional to
enzyme concentration. In contrast, neither the rate nor the extent of
hydrolysis of single-stranded DNA nor ATP is affected by high
concentrations of ATP. The amount of large single-stranded polynucleotide
generated by the action of the recBC DNase increases as the ATP
concentration increases and, at 0.5 mM ATP, becomes equivalent to the
amount of acid-soluble nucleotide formed. These findings suggest that high
intracellular concentrations of ATP affect the mechanism of the recBC DNase
so as to limit the extent of hydrolysis of duplex DNA, while at the same
time favoring the formation of single-stranded regions within the duplex.
Such regions may be essential intermediates in the recombination process.
On the role of ATP in phosphodiester bond hydrolysis catalyzed by the recBC deoxyribonuclease of Escherichia coli
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