available immediately in the group of Prof. Dr. Dagmar Klostermeier at the University of Münster, Institute for Physical Chemistry in the DFG-funded project “Mechanism of positive DNA supercoiling by reverse gyrase” (SFB 858). Reverse gyrase is a DNA topoisomerase unique to thermophilic and hyperthermophilic organisms that catalyses positive DNA supercoiling in an ATP-dependent reaction. The enzyme consists of a helicas-like domain, fused to a topoisomerase domain. Positive DNA supercoiling requires the intimate cooperation of the two domains, but the mechanism of their functional cooperation is not well understood.
Methoden:
You will investigate the molecular basis for the functional cooperation of the two domains in reverse gyrase using an array of biochemical and biophysical techniques, including single molecule fluorescence microscopy. The group has a state-of the art molecular biology and biochemistry laboratory plus confocal single molecule microscopes with alternating laser excitation and avalanche photodiode detectors, and total internal reflection microscopes with a fast CCD detection system.
Anfangsdatum: 1. Januar 2012
geschätzte Dauer: 3 Jahre
Bezahlung: 13 TV-L/2
Veröffentlichungen:
The conformational flexibility of the helicase-like domain from Thermotoga maritima reverse gyrase is restricted by the topoisomerase domain. del Toro Duany Y, Klostermeier D, Rudolph MG. Biochemistry. 2011 Jul 5;50(26):5816-23.
Nucleotide-driven conformational changes in the reverse gyrase helicase-like domain couple the nucleotide cycle to DNA processing. del Toro Duany Y, Klostermeier D. Phys Chem Chem Phys. 2011 Jun 7;13(21):10009-19.
The latch modulates nucleotide and DNA binding to the helicase-like domain of Thermotoga maritima reverse gyrase and is required for positive DNA supercoiling. Ganguly A, Del Toro Duany Y, Rudolph MG, Klostermeier D. Nucleic Acids Res. 2011 Mar;39(5):1789-800.
Homepage: http://www.uni-muenster.de/Chemie.pc/klostermeier/research.html
Applicants hold a Ph.D. in biochemistry, biophysics, or related fields and have a genuine interest in research and experimental enthusiasm. Experience in the preparation of proteins and nucleic acids, as well as molecular biology and biochemical methods, is required. Previous experience with single molecule spectroscopy is advantageous.
Applications of women are specially invited. In the case of similar qualification, competence and specific achievements, women will be considered on preferential terms within the framework of the legal possibilities. Handicapped candidates with equivalent qualifications will be given preference.
If you want to work in a stimulating environment as part of an international and interdisciplinary team, please send your application including CV, list of publications, letter of motivation, and two references to Prof. Dr. Dagmar Klostermeier, University of Muenster, Institute for Physical Chemistry, Corrensstr. 28/30, 48149 Münster, or to dagmar.klostermeier@uni-muenster.de. For informal inquiries, please contact dagmar.klostermeier@uni-muenster.de.