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M101594200v1
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Papers In Press, published online ahead of print April 3, 2001
J. Biol. Chem, 10.1074/jbc.M101594200
Submitted on February 20, 2001
Revised on April 2, 2001
Accepted on April 2, 2001

Stimulation of hNth1 by YB-1 (DbpB): Interaction between a base excision repair enzyme and a transcription factor

Dina R. Marenstein, Maria T.A. Ocampo, Michael K. Chan, Alvin Altamirano, Ashis K. Basu, Robert J. Boorstein, Richard P. Cunningham, and George W. Teebor

Department of Pathology, NYU School of Medicine, New York, NY 10016

Corresponding Author: george.teebor{at}med.nyu.edu

Human endonuclease III (hNth1) is a DNA Glycosylase / AP lyase which initiates base excision repair of pyrimidines modified by reactive oxygen species, ionizing and ultraviolet radiation. Using duplex 2'-deoxyriboseoligonucleotides 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 Ogg1 which are also members of the endonuclease III family. This difference in rates contrasts with the equality of rates found in E. coli and S. cerevisiae endonuclease III homologs. A yeast 2 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). In vitro addition of (His)6YB-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 non-covalent ES intermediate containing the AP aldehydic sugar and the epsilon -amino group of the hNth1 active site lysine. This equilibrium may be a checkpoint in modulating hNth1 activity.


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