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PMID: 2541429 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 86 ·No. 9 ·1989-05-00 ·Pages 3080-4

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

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.

MeSH Terms
Animals Buffers Cattle Chickens DNA/metabolism DNA Topoisomerases, Type I/metabolism DNA, Superhelical/metabolism Immunoglobulin kappa-Chains/genetics Kinetics Nucleic Acid Conformation Plants/enzymology Promoter Regions, Genetic Structure-Activity Relationship Substrate Specificity Temperature Triticum
Chemicals
Buffers DNA, Superhelical Immunoglobulin kappa-Chains DNA DNA Topoisomerases, Type I
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Camilloni G
Centro Acidi Nucleici, Consiglio Nazionale della Ricerche, Rome, Italy.
Di Martino E
Di Mauro E
Caserta M
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.86.9.3080
Published
1989-05-00
Pages
3080-4
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC287068
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.86.9.3080 PMC Full Text View journal details
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