Keywords :
Escherichia coli Proteins; Phosphates; Phosphorus Radioisotopes; DNA; DNA Polymerase I; Endodeoxyribonucleases; Deoxyribonuclease IV (Phage T4-Induced); endonuclease IV, E coli; DNA-(Apurinic or Apyrimidinic Site) Lyase; DNA/metabolism; DNA Polymerase I/metabolism; Endodeoxyribonucleases/metabolism; Escherichia coli/enzymology; Phosphates/metabolism; Substrate Specificity; Cell Biology; Genetics; Molecular Biology; Biochemistry; Structural Biology; Biophysics
Abstract :
[en] The 3' AP endonucleases (class I) are said to hydrolyze the phosphodiester bond 3' to AP sites yielding 3'-OH and 5'-phosphate ends; on the other hand, the resulting 3' terminal AP site is not removed by the 3'-5' exonuclease activity of the Klenow fragment [1]. We show that AP sites in DNA are easily removed by the 3'-5' exonuclease activity of the Klenow fragment and that they are excised as deoxyribose-5-phosphate. It is suggested that the 3' AP endonucleases are perhaps not the hydrolases they are supposed to be.
Scopus citations®
without self-citations
15
