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PMID: 266716 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Role of DNA gyrase in phiX replicative-form replication in vitro.

Marians KJ, Ikeda JE, Schlagman S, Hurwitz J

Abstract

Preparations containing DNA gyrase activity Gellert, M., Mizuchi, K., O'Dea, M.H. & Nash, H.A. (1976) Proc. Natl. Acad. Sci. USA 73, 3872-3876] have been extensively purified from Escherichia coli. Such fractions, in the presence of ATP and Mg2+, catalyze supertwisting of relaxed circular double-stranded DNA replicative forms of a number of DNAs that results in the formation of superhelical replicative forms. Relaxed phiX174 replicative form (phiX RFIV) is not attacked by the A protein endonuclease coded for by the phiX DNA genome. After exposure to preparations of DNA gyrase, the relaxed phiX174 replicative form is converted to phiX RFI which can then be attacked by the phiX gene A protein and participate in replication of duplex phiX DNA.

MeSH Terms
Adenosine Triphosphate/metabolism Coliphages/enzymology,metabolism DNA, Bacterial DNA, Circular DNA, Viral Magnesium/metabolism Novobiocin/pharmacology Nucleic Acid Conformation Viral Proteins/metabolism Virus Replication
Chemicals
DNA, Bacterial DNA, Circular DNA, Viral Viral Proteins Novobiocin Adenosine Triphosphate Magnesium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Marians K J
Ikeda J E
Schlagman S
Hurwitz J
References (18)
18 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
Published
1977-05-00
Pages
1965-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC431053
Subset
IM
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