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J Biol Chem, Vol. 275, Issue 11, 8103-8113, March 17, 2000

Roles of Topoisomerases in Maintaining Steady-state DNA Supercoiling in Escherichia coli*

E. Lynn Zechiedrichabc, Arkady B. Khodurskybef, Sophie Bachellierghi, Robert Schneiderjk, Dongrong Chengh, David M. J. Lilleygh, and Nicholas R. Cozzarellibd

From the a Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas 77030, the b Department of Molecular and Cell Biology, and e Biophysics Group, University of California, Berkeley, California 94720-3204, g Cancer Research Campaign Nucleic Acid Structure Research Group, Department of Biochemistry, University of Dundee, Dundee DD1 4HN United Kingdom, and the j Institut fur Genetik und Mikrobiologie, Ludwig Maximilian University, D-80638 München, Germany

DNA supercoiling is essential for bacterial cell survival. We demonstrated that DNA topoisomerase IV, acting in concert with topoisomerase I and gyrase, makes an important contribution to the steady-state level of supercoiling in Escherichia coli. Following inhibition of gyrase, topoisomerase IV alone relaxed plasmid DNA to a final supercoiling density (sigma ) of -0.015 at an initial rate of 0.8 links min-1. Topoisomerase I relaxed DNA at a faster rate, 5 links min-1, but only to a sigma  of -0.05. Inhibition of topoisomerase IV in wild-type cells increased supercoiling to approximately the same level as in a mutant lacking topoisomerase I activity (to sigma  = -0.08). The role of topoisomerase IV was revealed by two functional assays. Removal of both topoisomerase I and topoisomerase IV caused the DNA to become hyper-negatively supercoiled (sigma  = -0.09), greatly stimulating transcription from the supercoiling sensitive leu-500 promoter and increasing the number of supercoils trapped by lambda  integrase site-specific recombination.

* This work was supported by National Institutes of Health Grant GM 31657 (to N. R. C.) and National Institutes on Environmental Health Sciences Grant ESO1890 (to E. L. Z. and N. R. C.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

c Special Fellow of the Leukemia Society of America. Currently supported by a Curtis Hankamer Research Award and a New Investigator Award in the Toxicological Sciences for the Burroughs Wellcome Fund. To whom correspondence may be addressed. Tel.: (713) 798-5126; Fax: (713) 798-7375; E-mail: elz@bcm.tmc.edu.

d To whom correspondence may be addressed. Tel.: (510) 642-5266; Fax (510) 643-1079; E-mail: ncozzare@socrates.berkeley.edu.

f Present address: Department of Biochemistry, Stanford University, Stanford, CA 94305.

h Supported by the Cancer Research Campaign and the Medical Research Council (Dundee).

i Fellow of the European Molecular Biology Organization.

k Supported by the Deutsche Forschungsgemeinschaft through SFB 190.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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