An exonuclease activity associated with DNA polymerase I of Micrococcus radiodurans

Abstract

An exonuclease activity is associated with one of three DNA polymerase in Micrococcus radiodurans. The nuclease activity co-sedimented with its DNA polymerase I of this bacterium on glycerol gradient centrifugation. Both activities show the same optimum pH and heat-inactivation kinetics. This nuclease hydrolyzes preferentially double-stranded DNA in an exonucleolytic manner from both ends of the duplex DNA. The products of hydrolysis are mostly deoxyribonucleoside 5'-monophosphate and no nucleosides are released into the acid-soluble fraction. Di- or other oligonucleotides are also produced but their relative amounts are constant during the time of incubation. The exonuclease activity requires Mg2+ and is inhibited by high concentrations of KCl as is DNA polymerase I of M. radiodurans.