An Endonuclease for Depurinated DNA in Escherichia coli B

Abstract

Escherichia coli B cells contain an endonuclease which hydrolyzes apurinic sites in DNA. The enzyme has been demonstrated in vitro by the action of E. coli B41 proteins on depurinated DNA. This endonuclease probably plays a role in the molecular mechanism of the delayed inactivation of the T7 coliphage treated by monofunctional alkylating agents, which has been shown to be dependent on depurination; this endonuclease could also be a repair enzyme necessary for the first step of the repair of DNA containing apurinic sites.