Iron homeostasis and iron-sulfur cluster assembly in Escherichia coli
© 2016 John Wiley & Sons, Inc. All rights reserved. Throughout evolution, organisms have adapted a set of dedicated proteins for iron-sulfur cluster biogenesis. Among the identified iron-sulfur cluster assembly proteins in Escherichia coli, IscA has a unique and strong iron-binding activity, and the iron-bound IscA can readily provide iron for iron-sulfur cluster assembly in proteins in vitro under aerobic conditions. IscA also has a high binding affinity for copper, and excess copper competes for the iron-binding sites in IscA and effectively blocks the IscA-mediated iron-sulfur cluster biogenesis. It is thus postulated that IscA may act as an iron chaperone to recruit intracellular iron and deliver iron for iron-sulfur cluster biogenesis under aerobic conditions.
Publication Source (Journal or Book title)
Stress and Environmental Regulation of Gene Expression and Adaptation in Bacteria
Ding, H. (2016). Iron homeostasis and iron-sulfur cluster assembly in Escherichia coli. Stress and Environmental Regulation of Gene Expression and Adaptation in Bacteria, 1, 203-214. https://doi.org/10.1002/9781119004813.ch17