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J. Biol. Chem., Vol. 276, Issue 24, 21242-21249, June 15, 2001
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From the Human endonuclease III (hNth1) is a DNA
glycosylase/apurinic/apyrimidinic (AP) lyase that initiates base
excision repair of pyrimidines modified by reactive oxygen species,
ionizing, and ultraviolet radiation. Using duplex 2'-deoxyribose
oligonucleotides containing an abasic (AP) site, a thymine glycol, or a
5-hydroxyuracil residue as substrates, we found the AP lyase activity
of hNth1 was 7 times slower than its DNA glycosylase activity, similar to results reported for murine and human 8-oxoguanine-DNA
glycosylase, which are also members of the endonuclease III
family. This difference in rates contrasts with the equality of rates
found in Escherichia coli and Saccharomyces
cerevisiae endonuclease III homologs. A yeast two-hybrid screen
for potential modulators of hNth1 activity revealed interaction with
the damage-inducible transcription factor Y box-binding protein 1 (YB-1), also identified as DNA-binding protein B (DbpB). The in
vitro addition of His6YB-1 to hNth1 increased the rate of DNA glycosylase and AP lyase activity. Analysis revealed that YB-1 affects the steady state equilibrium between the covalent hNth1-AP site Schiff base ES intermediate and the noncovalent ES
intermediate containing the AP aldehydic sugar and the Department of Pathology and Kaplan
Comprehensive Cancer Center, New York University School of Medicine,
New York, New York 10016, the § Department of Chemistry,
University of Connecticut, Storrs, Connecticut 06269, and
¶ Department of Biological Sciences, The University at Albany,
SUNY, Albany, New York 12222
-amino group
of the hNth1 active site lysine. This equilibrium may be a checkpoint
in modulating hNth1 activity.
To whom correspondence should be addressed: Dept. of
Pathology, New York University Medical Center, 550 First Ave., New
York, NY 10016. Tel.: 212-263-5473; Fax: 212-263-8211; E-mail:
george.teebor@med.nyu.edu.
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