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J Biol Chem, Vol. 273, Issue 23, 14322-14330, June 5, 1998

DNA Ligase I Selectively Affects DNA Synthesis by DNA Polymerases  and  Suggesting Differential Functions in DNA Replication and Repair

From the Institute of Veterinary Biochemistry, University of Zürich-Irchel, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland

The joining of single-stranded breaks in double-stranded DNA is an essential step in many important processes such as DNA replication, DNA repair, and genetic recombination. Several data implicate a role for DNA ligase I in DNA replication, probably coordinated by the action of other enzymes and proteins. Since both DNA polymerases  and  show multiple functions in different DNA transactions, we investigated the effect of DNA ligase I on various DNA synthesis events catalyzed by these two essential DNA polymerases. DNA ligase I inhibited replication factor C-independent DNA synthesis by polymerase . Our results suggest that the inhibition may be due to DNA ligase I interaction with proliferating cell nuclear antigen (PCNA) and not to a direct interaction with the DNA polymerase  itself. Strand displacement activity by DNA polymerase  was also affected by DNA ligase I. The DNA polymerase  holoenzyme (composed of DNA polymerase , PCNA, and replication factor C) was inhibited in the same way as the DNA polymerase  core, strengthening the hypothesis of a PCNA interaction. Contrary to DNA polymerase , DNA synthesis by DNA polymerase  was stimulated by DNA ligase I in a PCNA-dependent manner. We conclude that DNA ligase I displays different influences on the two multipotent DNA polymerases and  through PCNA. This might be of importance in the selective involvement in DNA transactions such as DNA replication and various mechanisms of DNA repair.

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