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Title: Effect of divalent and monovalent cations on calf thymus PCNA-independent DNA polymerase delta and its 3'----5' exonuclease. Author: Focher F, Verri A, Maga G, Spadari S, Hübscher U. Journal: FEBS Lett; 1990 Jan 01; 259(2):349-52. PubMed ID: 1967165. Abstract: Recent data suggest that DNA polymerases alpha and delta might have a coordinate functional role at the replication fork. In this communication we show that Mg2+ is likely the natural metal activator for both enzymes. Mn2+, a known mutagenic agent, is a competitive inhibitor of Mg2+ for DNA polymerase delta and acompetitive for DNA polymerase alpha. The 3'----5' exonuclease activity associated with DNA polymerase delta is not affected upon addition of Mn2+. Be2+, another mutagenic agent, on the other hand, has an inhibitory effect on the 3'----5' exonuclease, but not on the DNA polymerase delta. The data presented might explain the mutagenic and carcinogenic potential of these two divalent cations.[Abstract] [Full Text] [Related] [New Search]