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Volume 272, Number 51, Issue of December 19, 1997
pp. 32230-32239
(Received for publication, July 3, 1997, and in revised form, September 25, 1997)
From the Department of Microbiology and Molecular Genetics, The
Markey Center for Molecular Genetics, The University of Vermont,
Burlington, Vermont 05405
Escherichia coli endonuclease VIII
(endo VIII) was identified as an enzyme that, like endonuclease III
(endo III), removes radiolysis products of thymine including thymine
glycol, dihydrothymine,
Characterization of Escherichia coli Endonuclease
VIII
-ureidoisobutyric acid, and urea from
double-stranded plasmid or phage DNA and cleaves the DNA strand at
abasic (AP) sites (Melamede, R. J., Hatahet, Z., Kow, Y. W.,
Ide., H., and Wallace, S. S. (1994) Biochemistry 33, 1255-1264). Using apparently homogeneous endo VIII protein, we now
show that endo VIII removes from double-stranded oligodeoxyribonucleotides the stable oxidative products of cytosine, 5-hydroxycytosine and 5-hydroxyuracil. Endo VIII cleaved the
damage-containing DNA strand by ,
-elimination as does
formamidopyrimidine DNA glycosylase (Fpg). Like Fpg, endo VIII also
excised the 5
-terminal deoxyribose phosphate from an endonuclease IV
(endo IV) pre-incised AP site. Thus, in addition to amino acid sequence
homology (Jiang, D., Hatahet, Z., Blaisdell, J., Melamede, R. J.,
and Wallace, S. S. (1997) J. Bacteriol. 179, 3773-3782), endo VIII shares a number of catalytic properties with
Fpg. In addition, endo VIII specifically bound to oligodeoxynucleotides
containing a reduced AP site with a stoichiometry of 1:1 for protein to
DNA with an apparent equilibrium dissociation constant of 3.9 nM. Like Fpg and endo III, the DNase I footprint was small
with contact sites primarily on the damage-containing strand; unlike
Fpg and endo III, the DNA binding of endo VIII to DNA was asymmetric,
3 to the reduced AP site.
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