The excision of AP sites by the 3'‐5' exonuclease activity of the Klenow fragment of Escherichia coli DNA polymerase I

FEBS Letters

Bailly, Véronique¹  Verly, Walter G.¹ 

[1] Laboratoire de Biochimie, Faculté des Sciences, Université de Liège, Sart Tilman B6, 4000 Liège I, Belgium

关键词: DNA repair;    AP site;    DNA polymerase I;    Klenow fragment;    3'-5'Exonuclease;    3'AP endonuclease;   

DOI  :  10.1016/0014-5793(84)80605-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown