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J. Biol. Chem., Vol. 275, Issue 40, 31399-31406, October 6, 2000
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From the Department of Pathology, Anatomy and Cell Biology, Thomas
Jefferson University, Philadelphia, Pennsylvania 19107
We reported that plant ribosome inactivating
proteins (RIP) have a unique DNA glycosylase activity that removes
adenine from single-stranded DNA (Nicolas, E., Beggs, J. M.,
Haltiwanger, B. M., and Taraschi, T. F. (1998) J. Biol. Chem. 273, 17216-17220). In this investigation, we further
characterized the interaction of the RIP gelonin with single-stranded
oligonucleotides and investigated its activity on double-stranded
oligonucleotides. At physiological pH, zinc and
Gelonin Is an Unusual DNA Glycosylase That Removes Adenine from
Single-stranded DNA, Normal Base Pairs and Mismatches*
-mercaptoethanol
stimulated the adenine DNA glycosylase activity of gelonin. Under these
conditions, gelonin catalytically removed adenine from single-stranded
DNA and, albeit to a lesser extent, from normal base pairs and
mismatches in duplex DNA. Also unprecedented was the finding that
activity on single-stranded and double-stranded oligonucleotides
containing multiple adenines generated unstable products with several
abasic sites, producing strand breakage and duplex melting,
respectively. The results from competition experiments suggested
similar interactions between gelonin's DNA-binding domain and
oligonucleotides with and without adenine. A re-examination of the
classification of gelonin as a DNA glycosylase/AP lyase using the
borohydride trapping assay revealed that gelonin was similar to the DNA
glycosylase MutY: both enzymes are monofunctional glycosylases, which
are trappable to their DNA substrates. The kcat
for the removal of adenine from single-stranded DNA was close to the
values observed with multisubstrate DNA glycosylases, suggesting that
the activity of RIPs on DNA may be physiologically relevant.
*
This work was supported in part by National Institutes of
Health Grant AI-41761.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Pathology,
Anatomy and Cell Biology, Thomas Jefferson University, JAH 229, 1020 Locust St., Philadelphia, PA 19107. Tel.: 215-503-5020; Fax:
215-955-5058; E-mail: Theodore.Taraschi@mail.tju.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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