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Nucleic Acids Research, 1981, Vol. 9, No. 4 909-920
© 1981

MOLECULAR BIOLOGY

DNA topoisomerase from Agrobacterium tumefaciens: purification and catalytic properties

Jeanne M. LeBon, Sudha Agarwal* and Jack G. Chirikjian

Department of Biochemistry, Georgetown University Medical Center Washington, DC 20007 *Bethesda Research Laboratories, Inc. Gaithersburg, MD 20850, USA

Received November 14, 1980. The DNA topoisomerase from Agrobacterium tumefaciens has been purified to apparent homogeneity. The enzyme is a single polypeptide of about 100,000 in molecular weight. No apparent separation of the nicking and sealing activities could be obtained in attempts to separate the two activities by a variety of methods, including limited protease digestion, thermal denaturation, and differential inhibition. Monoclonal antibodies obtained from hybridomas likewise did not preferentially inhibit one of the two activities. These results suggest that the two catalytic functions are carried by the same essential residues of the active enzyme site.


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