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 and genetic approaches. In particular, we determined the biochemical properties of HP0231 as well as its redox state in H. pylori cells.
Conclusion:
Altogether our results show that HP0231 is an oxidoreductase that catalyzes disulfide bond formation in the periplasm. We propose to call it HpDsbA.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Genetic Complementation Test
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Helicobacter pylori / enzymology*
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Helicobacter pylori / genetics
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Microscopy, Electron, Transmission
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Mutagenesis
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Oxidoreductases / metabolism*
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Plasmids
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Reverse Transcriptase Polymerase Chain Reaction
Grants and funding
The electron microscopy studies were performed in the Laboratory of Electron Microscopy, Nencki Institute of Experimental Biology, Warsaw, Poland by using electron microscope JEM1400 (JEOL Co., Japan, 2008) equipped with an energy-dispersive full range X-ray microanalysis system (EDS INCA Energy TEM, Oxford Instruments, Great Britain), a tomographic holder equipment and a high resolution digital camera (CCD MORADA, SiSOlympus, Germany). The above mentioned equipment was installed within the project sponsored by the European Union Structural Funds: Centre of Advanced Technology BIM - Equipment purchase for the Laboratory of Biological and Medical Imaging. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.