RELEASE OF 5'-TERMINAL DEOXYRIBOSE-PHOSPHATE RESIDUES FROM INCISED ABASIC SITES IN DNA BY THE ESCHERICHIA-COLI RECJ PROTEIN

被引:92
作者
DIANOV, G
SEDGWICK, B
DALY, G
OLSSON, M
LOVETT, S
LINDAHL, T
机构
[1] IMPERIAL CANC RES FUND,CLARE HALL LABS,S MIMMS EN6 3LD,HERTS,ENGLAND
[2] BRANDEIS UNIV,ROSENSTIEL BASIC MED SCI RES CTR,WALTHAM,MA 02254
[3] GOTHENBURG UNIV,SCH MED,DEPT MED BIOCHEM,S-40033 GOTHENBURG,SWEDEN
关键词
D O I
10.1093/nar/22.6.993
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.coli recJ strains were deficient in dRpase activity. The hydrolytic dRpase function of the RecJ protein requires Mg2+; in contrast, 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 function of DNA polymerase I, are unable to act as a dRpase. Nevertheless, E.coli fpg recJ double mutants retain capacity to repair abasic sites in DNA, indicating the presence of a back-up excision function.
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页码:993 / 998
页数:6
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