Title Experimental and Computational Characterization of the Ferric Uptake Regulator from Aliivibrio salmonicida (Vibrio salmonicida)
Author Hege Lynum Pedersen1, Rafi Ahmad1, Ellen Kristin Riise2,3, Hanna-Kirsti Schrøder Leiros2, Stefan Hauglid2, Sigrun Espelid1,2, Bjørn Olav Brandsdal2,3,4, Ingar Leiros2,3, Nils-Peder Willassen1,2, and Peik Haugen1,2*
Address 1Department of Molecular Biotechnology, Institute of Medical Biology, Faculty of Medicine, University of Tromsø, N-9037, Norway, 2The Norwegian Structural Biology Centre, University of Tromsø, N-9037, Norway, 3Department of Chemistry, Faculty of Science, University of Tromsø, N-9037, Norway, 4The Centre for Theoretical and Computational Chemistry, University of Tromsø, N-9037, Norway
Bibliography Journal of Microbiology, 48(2),174-183, 2010,
Key Words ferric uptake regulator, Fur, iron homeostasis, A. salmonicida, V. salmonicida
Abstract The Ferric uptake regulator (Fur) is a global transcription factor that affects expression of bacterial genes in an iron-dependent fashion. Although the Fur protein and its iron-responsive regulon are well studied, there are still important questions that remain to be answered. For example, the consensus Fur binding site also known as the “Fur box” is under debate, and it is still unclear which Fur residues directly interact with the DNA. Our long-term goal is to dissect the biological roles of Fur in the development of the disease cold-water vibriosis, which is caused by the psychrophilic bacteria Aliivibrio salmonicida (also known as Vibrio salmonicida). Here, we have used experimental and computational methods to characterise the Fur protein from A. salmonicida (AS-Fur). Electrophoretic mobility shift assays show that AS-Fur binds to the recently proposed vibrio Fur box consensus in addition to nine promoter regions that contain Fur boxes. Binding appears to be dependent on the number of Fur boxes, and the predicted “strength” of Fur boxes. Finally, structure modeling and molecular dynamics simulations provide new insights into potential AS-Fur–DNA interactions.