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JBC, Vol. 252, Issue 9, 2808-2814, May, 1977
S. Ljungquist
A new DNA endonuclease has been purified 3000-fold from Escherichia coli.
The enzyme specifically catalyzes the formation of single strand breaks at
apurinic and apyrimidinic sites in DNA, but has no activity on intact or
single-stranded DNA. Further, the enzyme shows little or no activity on
heavily ultraviolet-irradiated DNA, but cleaves x-irradiated DNA,
presumably at apurinic and apyrimidinic sites introduced by the radiation
treatment. The enzyme, which is tentatively named endonuclease IV, has no
detectable associated exonuclease or DNA N-glycosidase activity and does
not seem to be identical with any previously known E. coli endonuclease.
Endonuclease IV has no Mg2+ requirement, and is fully active in the
presence of EDTA. Enzyme activity is stimulated by 0.2 to 0.3 M NaCl and is
unusually salt-resistant. Further, the enzyme is fairly heat-stable, and is
not inhibited by tRNA. The sidimentation coefficient, S(o)20,w, is 3.4 S.
It seems that endonuclease IV is active in DNA repair.
A new endonuclease from Escherichia coli acting at apurinic sites in DNA
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