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(Received for publication, September 3, 1996)
From the Division of Cancer Biology, Department of Radiation
Oncology, Emory University School of Medicine, Atlanta, Georgia
30335
Deoxyinosine 3
Volume 271, Number 48,
Issue of November 29, 1996
pp. 30672-30676
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
-Endonuclease from Escherichia
coli
-endonuclease, an
Escherichia coli repair enzyme that recognizes and cleaves
DNA containing deoxyinosine and base mismatches, can cleave
heteroduplexes containing a hairpin or unpaired loop. These DNA
structures, referred to as insertion/deletion mismatches (IDM), are
abnormal intermediate structures generated during replication of
repetitive DNA sequences. In addition, the enzyme also cleaved the
5
-single-stranded tails of flap and pseudo-Y DNA structures,
suggesting that deoxyinosine 3
-endonuclease is a bacterial functional
homologue of human FEN1 and yeast RTH1 nucleases. These biochemical
properties suggest that deoxyinosine 3
-endonuclease might be important
in the repair of IDM structures generated in lagging strand during DNA
replication.
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