Nucleic Acids Research, Vol 24, Issue 22 4572-4576, Copyright © 1996 by Oxford University Press
T Shida, M Noda and J Sekiguchi
The Escherichia coli exonuclease III (AP endonuclease VI) is a DNA- repair
enzyme that hydrolyzes the phosphodiester bond 5' to an abasic site in DNA.
To study how the enzyme recognizes the abasic site, we used
oligonucleotides containing a synthetic abasic site at any desired position
in the sequence. We prepared oligonucleotides containing an abasic residue
such as 2'-deoxyribosylformamide, 2'-deoxyribose, 1',2'- dideoxy
ribofuranose or propanediol. Duplex oligonucleotides containing an abasic
residue used in this study were cleaved on the 5' side of the abasic site
by exonuclease III in spite of the varieties of the bases opposite and
adjacent to the abasic site. In addition, we observed that the enzyme
cleaved single-stranded oligonucleotides containing an abasic site on the
5' side of the abasic site. These findings suggest that the enzyme may
principally recognize the DNA-pocket formed at an abasic site. The indole
ring of the tryptophan 212 residue of the exonuclease III is probably
intercalated to the abasic site. The tryptophan in the vicinity of the
catalytic site is conserved in the type II AP endonuclease from various
organisms.
ARTICLES
Cleavage of single- and double-stranded DNAs containing an abasic residue by Escherichia coli exonuclease III (AP endonuclease VI)
Department of Applied Biology, Faculty of Textile Science and Technology, Shinshu University, Nagano, Japan. shida@pterus.shinshu- u.ac.jp
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