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PMID: 6265921 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

DNA breakage and closure by rat liver type 1 topoisomerase: separation of the half-reactions by using a single-stranded DNA substrate.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 78 ·No. 5 ·1981-05-00 ·Pages 2883-7

Been MD, Champoux JJ

Abstract

Circular single strands of bacteriophage phi X174 DNA are broken by rat liver DNA nicking-closing enzyme (type 1 topoisomerase) in low salt (50 mM KCl) at 37 degrees C, generating linear strands containing covalently bound enzyme [Been, M. D. & Champoux, J. J. (1980) Nucleic Acids Res. 8, 6129-6142]. The linear strands can be recircularized in the presence of 10 mM MgCl2 at 24 degrees C and 37 degrees C or 250 mM KCl at 24 degrees C. Recircularization is blocked when the hydroxyl group at the 5' terminus is phosphorylated. The linears generated by the nicking-closing enzyme can also be joined to other DNA fragments containing 5' hydroxyls, but not 5' phosphates. The linkage formed in both the intrastrand and interstrand reactions is stable to alkali. Reclosure of broken single strands is presumed to be analogous to the closure step that occurs durng nicking and closing cycles on duplex DNA.

MeSH Terms
Animals Bacteriophage phi X 174 DNA Helicases/metabolism DNA Topoisomerases, Type I/metabolism DNA, Single-Stranded/metabolism DNA, Viral/metabolism Kinetics Liver/enzymology Rats Substrate Specificity
Chemicals
DNA, Single-Stranded DNA, Viral DNA Helicases DNA Topoisomerases, Type I
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Been M D
Champoux J J
References (27)
27 references, click to expand
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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.78.5.2883
Published
1981-05-00
Pages
2883-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC319463
Subset
IM
Grants
NIGMS NIH HHS · GM23224 · United States
External Links
PubMed source DOI: 10.1073/pnas.78.5.2883 PMC Full Text View journal details
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