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Microbiology 150 (2004), 641-647; DOI  10.1099/mic.0.26867-0
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Microbiology 150 (2004), 641-647; DOI  10.1099/mic.0.26867-0
© 2004 Society for General Microbiology

Identification of a topoisomerase IV in actinobacteria: purification and characterization of ParYR and GyrBR from the coumermycin A1 producer Streptomyces rishiriensis DSM 40489

Elisabeth Schmutz, Susanne Hennig, Shu-Ming Li and Lutz Heide

Eberhard-Karls-Universität Tübingen, Pharmazeutische Biologie, Auf der Morgenstelle 8, D-72076 Tübingen, Germany

Correspondence
Lutz Heide
heide{at}uni-tuebingen.de
Shu-Ming Li
shuming.li{at}uni-tuebingen.de

The biosynthetic gene clusters of the gyrase inhibitors coumermycin A1 and clorobiocin contain two different resistance genes (gyrBR and parYR). Both genes code for B subunits of type II topoisomerases. The authors have now overexpressed and purified the encoded proteins, as well as the corresponding A subunits GyrA and ParX. Expression was carried out in Streptomyces lividans in the form of hexahistidine fusion proteins, allowing purification by nickel affinity chromatography. The complex of GyrA and GyrBR was found to catalyse ATP-dependent supercoiling of DNA, i.e. to function as a gyrase, whereas the complex of ParX and ParYR catalysed ATP-dependent decatenation and relaxation, i.e. the functions of topoisomerase IV (topo IV). This is believed to represent the first topo IV identified in the class of actinobacteria, and the first demonstration of the formation of a topo IV as a resistance mechanism of an antibiotic producer.

Abbreviations: kDNA, kinetoplast DNA; topo IV, topoisomerase IV




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