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In vivo evidence for the iron binding activity of an iron-sulfur cluster assembly protein IscA in Escherichia coli |
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Τρίτη, 12 Οκτώβριος 2010 17:00 |
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IscA is a key member of the iron-sulfur cluster assembly machinery in prokaryotic and eukaryotic organisms. However, the physiological function of IscA still remains elusive. Here we report the in vivo evidence demonstrating the iron binding activity of IscA in Escherichia coli cells. Supplement of exogenous iron (1 µM) in the M9 minimal medium is sufficient to maximize the iron binding in IscA expressed in E. coli cells under aerobic growth conditions. In contrast, IscU, an iron-sulfur cluster assembly scaffold protein, or CyaY, a bacterial frataxin homologue, fails to bind any iron in E. coli cells under the same experimental conditions. Interestingly, the strong iron binding activity of IscA is greatly diminished in E. coli cells under anaerobic growth conditions. Additional stud...MedWorm Message: Watch the new MedWorm demo and find out how to get all the very latest, relevant, organized information daily!
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