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Regulation of the function of eukaryotic DNA topoisomerase I: topological conditions for inactivity.

By G Camilloni, E Di Martino, E Di Mauro and M Caserta

Abstract

The effects of supercoiling on the cleavage reaction by eukaryotic DNA topoisomerases I (wheat germ, chicken erythrocyte, and calf thymus) have been analyzed on DNA fragments (0.96 and 2.3 kilobases) encompassing an immunoglobulin kappa light-chain promoter. In one topological condition of the substrate, the absolutely relaxed state, cleavage was found to be impeded. This finding defines the topology-dependent step of the eukaryotic DNA topoisomerase I reaction and shows that for the cleavage reaction topology is more critical than sequence effects. These findings suggest a simple model for the regulation of the DNA topoisomerase I reaction based on topological factors, which may explain the regulatory function of the enzyme in in vivo eukaryotic transcription

Topics: Research Article
Year: 1989
OAI identifier: oai:pubmedcentral.nih.gov:287068
Provided by: PubMed Central
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