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(Received for publication, July 17, 1996, and in revised form, September 4, 1996)
From the Departments of Repair of abasic lesions, one of the most common
types of damage found in DNA, is crucial to an organism's
well-being. Studies in vitro indicate that after
apurinic-apyrimidinic endonuclease cleaves immediately upstream of a
baseless site, removal of the 5 Eukaryotic RAD2 homolog 1 (RTH1) nuclease, by genetic and biochemical
evidence, is involved in repair of modified DNA. Efficient endonucleolytic cleavage by RTH1 nuclease has been demonstrated for
annealed primers that have unannealed 5
Volume 271, Number 47,
Issue of November 22, 1996
pp. 30068-30076
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
- to 3-Exo/Endonuclease Can Efficiently
Excise a Displaced DNA Fragment Containing a 5-Terminal Abasic
Lesion by Endonuclease Activity
,
and
Biochemistry and
Ophthalmology, University of Rochester School of Medicine and
Dentistry, Rochester, New York 14642 and § Life Science
Division, Los Alamos National Laboratory,
Los Alamos, New Mexico 87545
-terminal sugar-phosphate residue is
achieved by deoxyribophosphodiesterase activity, an enzyme-mediated
-elimination reaction, or by endonucleolytic cleavage downstream of
the baseless sugar. Synthesis and ligation complete repair.
-tails. In vivo,
such substrate structures could result from repair-related strand
displacement synthesis. Using 5-tailed substrates, we examined the
ability of human RTH1 nuclease to efficiently remove 5-terminal abasic residues. A series of upstream primers were used to increasingly displace an otherwise annealed downstream primer containing a 5-terminal deoxyribose-5-phosphate. Until displacement of the first
annealed nucleotide, substrates resisted cleavage. With further
displacement, efficient cleavage occurred at the 3-end of the tail.
Therefore, in combination with strand displacement activity, RTH1
nucleases may serve as an important alternative to other pathways in
repair of abasic sites in DNA.
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