A novel insight into the oxidoreductase activity of Helicobacter pylori HP0231 protein.
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.


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 and genetic approaches. In particular, we determined the biochemical properties of HP0231 as well as its redox state in H. pylori cells.


CONCLUSIONS
Altogether our results show that HP0231 is an oxidoreductase that catalyzes disulfide bond formation in the periplasm. We propose to call it HpDsbA.
Department of Bacterial Genetics, Institute of Microbiology, the University of Warsaw, Warsaw, Poland.
Paula
P
Roszczenko
Katarzyna A
KA
Radomska
Ewa
E
Wywial
Jean-Francois
JF
Collet
Elzbieta K
EK
Jagusztyn-Krynicka
D005816:Genetic Complementation Test; D016480:Helicobacter pylori / Q000201:enzymology* / Q000235:genetics; D046529:Microscopy, Electron, Transmission; D016296:Mutagenesis; D010088:Oxidoreductases / Q000378:metabolism*; D010957:Plasmids; D020133:Reverse Transcriptase Polymerase Chain Reaction
D010088:Oxidoreductases