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J. Biol. Chem., Vol. 266, Issue 34, 22893-22898, Dec, 1991
JD Levin, R Shapiro and B Demple
Escherichia coli endonuclease IV and its Saccharomyces cerevisiae homologue
Apn1, two DNA repair enzymes for free radical damages, were previously
shown to be inactivated by metal-chelating agents. In the present study,
atomic absorption spectrometry of endonuclease IV revealed the presence of
2.4 zinc and 0.7 manganese atoms, whereas Apn1 contained 3.3 zinc atoms and
no significant manganese. EDTA-inactivated endonuclease IV retained 0.7
zinc atom but little detectable manganese. ZnCl2 reactivated
1,10-phenanthroline-treated Apn1, but was ineffective with endonuclease IV
treated with either 1,10-phenanthroline or EDTA. In contrast, enzymatic
activity was restored to both enzymes after EDTA treatment by incubation
with CoCl2 and to a lesser extent by MnCl2. Endonuclease IV, reactivated
with CoCl2 or MnCl2, regained all of the activities characteristic of the
native enzyme. MnCl2 was as effective as CoCl2 at restoring activity to the
1,10-phenanthroline-treated enzymes. The results indicate that intrinsic
metals play critical roles in both endonuclease IV and Apn1 and that
manganese may perform a special function in endonuclease IV. Possible
mechanistic roles for the metals in these DNA repair enzymes are discussed.
Metalloenzymes in DNA repair. Escherichia coli endonuclease IV and Saccharomyces cerevisiae Apn1
Department of Molecular and Cellular Toxicology, Harvard School of Public Health, Boston, Massachusetts 02115.
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