Journal
FREE RADICAL RESEARCH
Volume 40, Issue 6, Pages 597-605Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1080/10715760600618882
Keywords
oxidative stress; Dps; Helicobacter; iron binding; DNA protection
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Funding
- NIDDK NIH HHS [DK62852, DK60061] Funding Source: Medline
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The ferritin-like DNA-binding protein from starved cells (Dps) family proteins are present in a number of pathogenic bacteria. Dps in the enterohepatic pathogen, Helicobacter hepaticus is characterized and a H. hepaticus dps mutant was generated by insertional mutagenesis. While the wild type H. hepaticus cells were able to survive in an atmosphere containing up to 6.0% O-2, the dps mutant failed to grow in 3.0% O-2, and it was also more sensitive to oxidative reagents like H2O2, cumene hydroperoxide and t-butyl hydroperoxide. Upon air exposure, the dps 2 cells had more damaged DNA than the wild type; they became coccoid or lysed and they contained similar to 6-fold higher amount of 8-oxoguanine (8-oxoG) DNA lesions than wild type cells. Purified H. hepaticus Dps was shown to be able to bind both iron and DNA. The iron-loaded form of Dps protein had much greater DNA binding ability than the native Dps or the iron-free Dps.
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