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A more recent version of this article appeared on July 15, 2005
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M502838200v1
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Papers In Press, published online ahead of print May 15, 2005
J. Biol. Chem, 10.1074/jbc.M502838200
Submitted on March 15, 2005
Revised on April 27, 2005
Accepted on May 15, 2005

A superhelical spiral in the Escherichia coli DNA gyrase A C-terminal domain imparts unidirectional supercoiling bias

Alexander J. Ruthenburg, Daina M. Graybosch, John C. Huetsch, and Gregory L. Verdine

Department of Chemistry, Chemical Biology, Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138

Corresponding Author: gregory_verdine{at}harvard.edu

DNA Gyrase is unique among topoisomerases in that its DNA supercoiling activity is unidirectional. The C-terminal domain of the GyrA subunit (GyrA-CTD) is required for this supercoiling bias. We report the X-ray structure of the Escherichia coli GyrA-CTD. The E. coli GyrA-CTD adopts a circular-shaped ß-pinwheel fold first seen in the Borrelia burgdorferi GyrA-CTD. However, whereas the B. burgdorferi GyrA-CTD is flat, the E. coli GyrA-CTD is spiral. DNA relaxation assays reveal that the E. coli GyrA-CTD wraps DNA inducing substantial (+) superhelicity, while the B. burgdorferi GyrA-CTD introduces a more modest (+) superhelicity. The observation of a superhelical spiral in the present structure and that of the Bacillus stearothermophilus ParC-CTD structure suggests unexpected similarities in substrate selectivity between Gyrase and Topo IV enzymes. We propose a model wherein the right-handed ((+) solenoidal) wrapping of DNA about the E. coli GyrA-CTD enforces unidirectional (-) DNA supercoiling.


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