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Journal of Bacteriology, May 1999, p. 3185-3192, Vol. 181, No. 10
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Escherichia coli DNA Topoisomerase I Copurifies with Tn5 Transposase, and Tn5 Transposase Inhibits Topoisomerase I

Hesna Yigitdagger and William S. Reznikoff*

Department of Biochemistry, University of Wisconsin---Madison, Madison, Wisconsin 53706

Received 16 September 1998/Accepted 13 March 1999

Tn5 transposase (Tnp) overproduction is lethal to Escherichia coli. Genetic evidence suggested that this killing involves titration of E. coli topoisomerase I (Topo I). Here, we present biochemical evidence that supports this model. Tn5 Tnp copurifies with Topo I while nonkilling derivatives of Tnp, Delta 37Tnp and Delta 55Tnp (Inhibitor [Inh]), show reduced affinity or no affinity, respectively, for Topo I. In agreement with these results, the presence of Tnp, but not Delta 37 or Inh derivatives of Tnp, inhibits the DNA relaxation activity of Topo I in vivo as well as in vitro. Other proteins, including RNA polymerase, are also found to copurify with Tnp. For RNA polymerase, reduced copurification with Tnp is observed in extracts from a topA mutant strain, suggesting that RNA polymerase interacts with Topo I and not Tnp.

* Corresponding author. Mailing address: Department of Biochemistry, 433 Babcock Dr., Madison, WI 53706-1544. Phone: (608) 262-3608. Fax: (608) 262-3453. E-mail: reznikoff{at}biochem.wisc.edu.

dagger Present address: Nosocomial Pathogens Laboratory Branch, Centers for Disease Control and Prevention, 1600 Clifton Rd., Mail Stop G08, Atlanta, GA 30333.

Journal of Bacteriology, May 1999, p. 3185-3192, Vol. 181, No. 10
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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