1887

Abstract

membrane-bound ferritin (MbfA) is a member of the erythrin (Er)–vacuolar iron transport family. The MbfA protein has an Er or ferritin-like domain at its N terminus and has been predicted to have five transmembrane segments in its C-terminal region. Analysis of protein localization using PhoA and LacZ reporter proteins supported the view that the N-terminal di-iron site is located in the cytoplasm whilst the C-terminal end faces the periplasm. An mutant strain had 1.5-fold higher total iron content than the WT strain. Furthermore, multi-copy expression of reduced total iron content two- and threefold in WT and mutant backgrounds, respectively. These results suggest that MbfA may function as an iron exporter rather than an iron storage protein. The mutant showed 10-fold increased sensitivity to the iron-activated antibiotic streptonigrin, implying that the mutant had increased accumulation of intracellular free iron. Growth of the mutant was reduced in the presence of high iron under acidic conditions. The expression of was induced highly in cells grown in iron-replete medium at pH 5.5, further supporting the view that is involved in the response to iron under acidic conditions. MbfA may play a protective role against increased free iron in the cytoplasm through iron binding and export, thus preventing iron-induced toxicity via the Fenton reaction.

Funding
This study was supported by the:
  • , Royal Golden Jubilee Scholarship , (Award PHD52K0207)
  • , Chulabhorn Research Institute
  • , Thailand Research Fund , (Award RSA5380004)
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2014-05-01
2021-03-06
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