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PMID: 198805 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Strand breakage by the DNA untwisting enzyme results in covalent attachment of the enzyme to DNA.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 74 ·No. 9 ·1977-09-00 ·Pages 3800-4

Champoux JJ

Abstract

Strands of DNA that have been broken by the DNA untwisting enzyme exhibit a reduced buoyant density in alkaline CsCl due to bound protein. A covalent linkage between the DNA and the enzyme was indicated by the stability of the complex in alkali (pH greaterthan 12.7), in 7 M guanidine-HCl, and at 90 degrees in 1% Sarkosyl for 5 min. The single-strand breaks generated by the enzyme are resistant to exonuclease III, indicating that the protein is attached to one of the ends of the broken strands. The free end of the broken strand bears a 5'-hydroxyl group, indicating attachment of the protein to the 3'-phosphoryl terminus. A nucleotide-peptide linkage involving a phosphoamide bond is unlikely since the complex is resistant to 3.5 M hydroxylamine at pH 4.75.

MeSH Terms
Animals Cell Nucleus/enzymology DNA Topoisomerases, Type I/metabolism DNA, Viral/metabolism Deoxyribonucleases Exonucleases Guanidines Hydroxylamines Liver/enzymology Protein Binding Rats Simian virus 40
Chemicals
DNA, Viral Guanidines Hydroxylamines Deoxyribonucleases Exonucleases DNA Topoisomerases, Type I
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Champoux J J
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26 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.74.9.3800
Published
1977-09-00
Pages
3800-4
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC431737
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.74.9.3800 PMC Full Text View journal details
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