Zinc is an essential metal that plays a structural or catalytic role in many cellular proteins. In response to zinc limitation, Streptomyces coelicolor produces a high affinity zinc uptake system (ZnuACB). Disruption of this system results in a ΔznuACB-zur mutant growing poorly in the absence of supplemental zinc, implying that the ZnuABC system is a key zinc uptake system for S. coelicolor. The Δzur mutant exhibited a sporulation defect, and appeared to inhibit sporulation of ΔznuA mutants, suggesting there might be cross-talk between the strains. Several important features are presented relating the structure of Zur to its function as a zinc-sensing regulatory protein and help differentiate Zur from the structurally similar iron uptake regulator, Fur. Zur was purified and the interaction between Zur and the promoter region of znuA investigated using electromobility shift assays (EMSA) and DNase I footprinting. SI nuclease digestion assays were used to investigate the role of Zur in controlling expression of znuA.
| Identifer | oai:union.ndltd.org:bl.uk/oai:ethos.bl.uk:494926 |
| Date | January 2009 |
| Creators | Pascoe, Ben |
| Publisher | University of Sussex |
| Source Sets | Ethos UK |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
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