Nucleic Acids Research, Vol 26, Issue 11 2593-2597, Copyright © 1998 by Oxford University Press
KM Shafritz, M Sandigursky and WA Franklin
The bacteria Escherichia coli contains several exonucleases acting on both
double- and single-stranded DNA and in both a 5'-->3' and 3'-->5'
direction. These enzymes are involved in replicative, repair and
recombination functions. We have identified a new exonuclease found in
E.coli, termed exonuclease IX, that acts preferentially on single- stranded
DNA as a 3'-->5' exonuclease and also functions as a 3'-
phosphodiesterase on DNA containing 3'-incised apurinic/apyrimidinic (AP)
sites to remove the product trans -4-hydroxy-2-pentenal 5- phosphate. The
enzyme showed essentially no activity as a deoxyribophosphodiesterase
acting on 5'-incised AP sites. The activity was isolated as a glutathione
S-transferase fusion protein from a sequence of the E.coli genome that was
60% identical to a 260 bp region of the small fragment of the DNA
polymerase I gene. The protein has a molecular weight of 28 kDa and is free
of AP endonuclease and phosphatase activities. Exonuclease IX is expressed
in E.coli , as demonstrated by reverse transcription-PCR, and it may
function in the DNA base excision repair and other pathways.
ARTICLES
Exonuclease IX of Escherichia coli
Department of Radiology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
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