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J. Biol. Chem., Vol. 269, Issue 22, 15498-15504, 06, 1994
YC Yeh, HF Liu, CA Ellis and AL Lu
The all-type nicking enzyme (ATE) from human HeLa cells or calf thymus can
nick DNA at the first phosphodiester bond 5' to all 8 possible mismatched
bases. The strand disparity of this nicking is influenced by the
neighboring nucleotide sequences. After nicking, the ATE covalently binds
to the 3' end of the DNA product to form a cleavable complex, whose
formation is insensitive to camptothecin, a specific inhibitor of
eukaryotic topoisomerase I (Topo-I). During the purification of ATE from
calf thymus, a Mg(2+)-independent relaxation activity, characteristic of
eukaryotic Topo-I, copurifies with the mismatch- nicking activity. The ATE
from calf thymus may be a breakdown product of Topo-I. N-terminal amino
acid analysis indicates that one of the polypeptides with ATE activity
contains the C-terminal portion of Topo- I. Moreover, active human Topo-I,
expressed as a fusion protein in Escherichia coli, is also capable of
nicking all 8 base mispairs in the absence of Mg2+. This mismatch-specific
nicking activity may be a novel property of the mammalian Topo-I.
Mammalian topoisomerase I has base mismatch nicking activity
Department of Biological Chemistry, University of Maryland, School of Medicine, Baltimore 21201.
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