Upregulation of a non-heme iron-containing ferritin with dual ferroxidase and DNA-binding activities in Helicobacter pylori under acid stress
| Autor: | Shyh-Horng Chiou, Chun-Hao Huang, I-Ju Yeh, Jiahn-Haur Liao, Shih-Hsiung Wu, I-Liang Lee, Chun Lun Ni |
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| Rok vydání: | 2009 |
| Předmět: |
Proteomics
Time Factors Protein Conformation Molecular Sequence Data Down-Regulation Ferroxidase activity Biochemistry chemistry.chemical_compound Bacterial Proteins Stress Physiological RNA Messenger Molecular Biology Polyacrylamide gel electrophoresis Heme chemistry.chemical_classification biology Helicobacter pylori Gene Expression Profiling Microchemistry Ceruloplasmin Computational Biology General Medicine Sequence Analysis DNA Hydrogen-Ion Concentration biology.organism_classification Molecular biology Adaptation Physiological Recombinant Proteins Up-Regulation Ferritin DNA-Binding Proteins Molecular Weight Enzyme chemistry Genes Bacterial Proteome Ferritins biology.protein DNA Damage |
| Zdroj: | Journal of biochemistry. 147(4) |
| ISSN: | 1756-2651 |
| Popis: | Helicobacter pylori is a spiral Gram-negative microaerophilic bacterium. It is unique and distinctive among various bacterial pathogens for its ability to persist in the extreme acidic environment of human stomachs. To address and identify changes in the proteome of H. pylori in response to low pH, we have used a proteomic approach to study the protein expression of H. pylori under neutral (pH 7) and acidic (pH 5) conditions. Global protein-expression profiles of H. pylori under acid stress were analysed by two-dimensional polyacrylamide gel electrophoresis (2-DE) followed by liquid chromatography (LC)-nanoESI-mass spectrometry (MS)/MS and bioinformatics database analysis. Among the proteins differentially expressed under acidic condition, a non-heme iron-containing ferritin of H. pylori (HP-ferritin) was found to be consistently upregulated at pH 5 as compared to pH 7. It was also found that HP-ferritin can switch from an iron-storage protein with ferroxidase activity to a DNA-binding/protection function under in vitro conditions upon exposure to acidic environment. Prokaryotic ferritins, such as non-heme iron-binding HP-ferritin with dual functionality reported herein, may play a significant urease-independent role in the acid adaptation of H. pylori under physiological conditions in vivo. |
| Databáze: | OpenAIRE |
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