DNA binding and antigenic specifications of DNA gyrase

descriptionPublicationkeyboard_double_arrow_right Article 01 Jan 1984 English Publisher:Oxford University Press (OUP)Journal:Nucleic Acids Research, volume 12, pages 901-914 (issn: 0305-1048, eissn: 1362-4962,

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Authors: H, Lother; R, Lurz; E, Orr;

doi: 10.1093/nar/12.2.901

pmid: 6198633

pmc: PMC318544

DNA binding and antigenic specifications of DNA gyrase

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Abstract

Complexes of DNA gyrase and minichromosomal DNA containing the origin of replication of Escherichia coli (oriC) can be formed without metabolic energy and visualised by electron microscopy. The A subunit, part of the A2B2-DNA gyrase complex is the binding protein. Various binding sites are scattered around the minichromosomal DNA including oriC. The minimal origin contains the only prominent and reproducible binding site. Binding to this site is suppressed by oxolinic acid and the ATP analogue beta-y-imido ATP. If gyrase isolated from the gram-positive bacterium Bacillus subtilis is used no binding to oriC is seen. This observation is consistent with antigenic differences between the A subunits of the two microorganisms. The binding to oriC might reflect a requirement for DNA gyrase during the initiation of DNA replication.

Related Organizations

University of Leicester
United Kingdom
Max Planck Institute for Molecular Genetics
Germany
Max Planck Society
Germany

Keywords

Base Sequence, Macromolecular Substances, Nucleic Acid Hybridization, Antigen-Antibody Complex, DNA, Substrate Specificity, Epitopes, Microscopy, Electron, DNA Topoisomerases, Type II, Escherichia coli, Bacillus subtilis, Protein Binding

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