PMID:9592142
| Citation |
Shafritz, KM, Sandigursky, M and Franklin, WA (1998) Exonuclease IX of Escherichia coli. Nucleic Acids Res. 26:2593-7 |
|---|---|
| Abstract |
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. |
| Links | |
| Keywords |
DNA, Single-Stranded/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Exodeoxyribonuclease V; Exodeoxyribonucleases/genetics; Exodeoxyribonucleases/isolation & purification; Exodeoxyribonucleases/metabolism; Gene Expression; Phosphoric Diester Hydrolases/genetics; Phosphoric Diester Hydrolases/isolation & purification; Phosphoric Diester Hydrolases/metabolism |
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