G. Dianov et al., RELEASE OF 5'-TERMINAL DEOXYRIBOSE-PHOSPHATE RESIDUES FROM INCISED ABASIC SITES IN DNA BY THE ESCHERICHIA-COLI RECJ PROTEIN, Nucleic acids research, 22(6), 1994, pp. 993-998
Excision of deoxyribose-phosphate residues from enzymatically incised
abasic sites in double-stranded DNA is required prior to gap-filling a
nd ligation during DNA base excision-repair, and a candidate deoxyribo
phosphodiesterase (dRpase) activity has been identified in E.coli. Thi
s activity is shown here to be a function of the E.coli RecJ protein,
previously described as a 5'-->3' single-strand specific DNA exonuclea
se 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 a
n overproducer strain had both 5'-->3' exonuclease and dRpase activity
. Moreover, E.coli recJ strains were deficient in dRpase activity. The
hydrolytic dRpase function of the RecJ protein requires Mg2+; in cont
rast, the activity of E.coli Fpg protein, that promotes the liberation
of 5'-->3' Rp residues from DNA by beta-elimination, is suppressed by
Mg2+. Several other E.coli nucleases, including exonucleases I, III,
V, and VII, endonucleases I, III and IV and the 5'-->3' exonuclease fu
nction of DNA polymerase I, are unable to act as a dRpase. Nevertheles
s, E.coli fpg recJ double mutants retain capacity to repair abasic sit
es in DNA, indicating the presence of a back-up excision function.