Nucleic Acids Research, 1994, Vol. 22, No. 6 993-998
© 1994
ENZYMOLOGY |
Release of 5'-terminal deoxyribose-phosphate residues from incised abasic sites in DNA by the Escherichia coli RecJ protein
Imperial Cancer Research Fund, Clare Hall Laboratories South Mimms, Hertfordshire EN6 3LD, UK 1Rosenstiel Basic Medical Sciences Research Center, Brandeis University Waltham, MA 02254-911, USA
* To whom correspondence should be addressed
Received December 22, 1993. Revised February 15, 1994. Accepted February 15, 1994.
Excision of deoxyribose-phosphate residues from enzymatically incised abasic sites in double-stranded DNA is required prior to gap-filling and ligation during DNA base excision-repair, and a candidate deoxyribophosphodiesterase (dRpase) activity has been identified in E.coli. This activity is shown here to be a function of the E.coli RecJ protein, previously described as a 5' - 3' single-strand specific DNA exonuclease involved in a recombination pathway and in mismatch repair. Highly purified preparations of dRpase contained 5'-3' exonuclease activity for single-stranded DNA, and homogeneous RecJ protein purified from an overproducer strain had both 5' - 3' exonuclease and dRpase activity. Moreover, E.coll recJ strains were deficient in dRpase activity. The hydrolytic dRpase function of the RecJ protein requires Mg2+; in contrast, the activity of E.coll Fpg protein, that promotes the liberation of 5' – 3' Rp residues from DNA by ß-eliminatlon, is suppressed by Mg2+. Several other E.coll nucleases, including exonucleases I, III, V, and VII, endonucleases I, III and IV and the 5' – 3' exonuclease function of DNA polymerase I, are unable to act as a dRpase. Nevertheless, E.coll fpg recJ double mutants retain capacity to repair abasic sites in DNA, indicating the presence of a back-up excision function.
+ Present address: Department of Pathology, University of Texas, Southwestern Medical Center at Dallas, TX 75235-9072. USA
Permanent address: Department of Medical Biochemistry, University of Gothenburg Medical School, 40033 Sweden
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