a novel insight into the oxidoreductase activity of helicobacter pylori hp0231 protein一种新颖的见解幽门螺杆菌hp0231蛋白质的氧化还原酶的活动.pdfVIP

A Novel Insight into the Oxidoreductase Activity of Helicobacter pylori HP0231 Protein 1,2 1 3 4,5,6 Paula Roszczenko , Katarzyna A. Radomska , Ewa Wywial , Jean-Francois Collet , Elzbieta K. Jagusztyn-Krynicka1* 1 Department of Bacterial Genetics, Institute of Microbiology, the University of Warsaw, Warsaw, Poland, 2 College of Inter-Faculty Individual Studies in Mathematics and Natural Sciences, the University of Warsaw, Warsaw, Poland, 3 Laboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology, ´ ´ Warsaw, Poland, 4 WELBIO (Walloon Excellence in Life Sciences and Biotechnology), Universite Catholique de Louvain, Brussels, Belgium, 5 de Duve Institute, Universite Catholique de Louvain, Brussels, Belgium, 6 Brussels Center for Redox Biology, Brussels, Belgium Abstract Background: The formation of a disulfide bond between two cysteine residues stabilizes protein structure. Although we now have a good understanding of the Escherichia coli disulfide formation system, the machineries at work in other bacteria, including pathogens, are poorly characterized. Thus, the objective of this work was to improve our understanding of the disulfide formation machinery of Helicobacter pylori, a leading cause of ulcers and a risk factor for stomach cancer worldwide. Methods and Results: The protein HP0231 from H. pylori, a structural counterpart of E. coli DsbG, is the focus of this research. Its function was clarified by using a combination of biochemical, microbiological a