a INRA, UR 546 Biostatistics and Spatial Processes, (BioSP), F-84914 Avignon, France b Mediterranean Institute of Oceanology, University of Aix-Marseille II, Parc Scientifique et Technologique de Luminy, Case 901, 13288 Marseille Cedex 9, France c Institute of Marine and Coastal Sciences, Rutgers University, 71 Dudley Rd, New Brunswick, NJ, USA d Université de la Nouvelle-Calédonie, Laboratoire...

The 2.7 A crystal structure of the 55-kDa N-terminal breakage-reunion domain of topoisomerase (topo) IV subunit A (ParC) from Streptococcus pneumoniae, the first for the quinolone targets from a gram-positive bacterium, has been solved and reveals a 'closed' dimer similar in fold to Escherichia coli DNA gyrase subunit A (GyrA), but distinct from the 'open' gate structure of Escherichia coli Par...

Background: Emergence Klebsiella pneumoniae resistant to quinolone antibiotics due to mutations in gyrA and parC genes created problem for treatment of patients in different hospitals in Iran. The objective of this study was to determine the amino acid substitutions of GyrA and ParC proteins in certain clonal lineages of the K. pneumoniae conferring high level quinolone resistance. Methods: One...

Prokaryotic chromosomes and plasmids encode partitioning systems that are required for DNA segregation at cell division. The systems are thought to be functionally analogous to eukaryotic centromeres and to play a general role in DNA segregation. The parA system of plasmid R1 encodes two proteins ParM and ParR, and a cis-acting centromere-like site denoted parC. The ParR protein binds to parC i...

Two different type II topoisomerases are known in bacteria. DNA gyrase (Gyr) introduces negative supercoils into DNA. Topoisomerase IV (Par) relaxes DNA supercoils. GyrA and ParC subunits of bacterial type II topoisomerases are involved in breakage and reunion of DNA. The spatial structure of the C-terminal fragment in GyrA/ ParC is not available. We infer homology between the C-terminal domain...

The Escherichia coli low-copy-number plasmid R1 contains a segregation machinery composed of parC, ParR and parM. The R1 centromere-like site parC contains two separate sets of repeats. By atomic force microscopy (AFM) we show here that ParR molecules bind to each of the 5-fold repeated iterons separately with the intervening sequence unbound by ParR. The two ParR protein complexes on parC do n...

The aim of this study was to examine mutations in the quinolone-resistance-determining region (QRDR) of gyrA and parC genes in Pseudomonas aeruginosa isolates. A total of 100 clinical P. aeruginosa isolates were collected from different university-affiliated hospitals in Tabriz, Iran. Minimum inhibitory concentrations (MICs) of ciprofloxacin and levofloxacin were evaluated by agar dilution assa...