Ferritin is an iron storage protein that plays an important role in maintaining intracellular iron homeostasis.  Ferritin expression is post-transcriptionally regulated by iron regulatory protein (IRP) via binding to the iron-responsive element (IRE), a 28-nucleotide hairpin stem-loop structure, in the 5’ untranslated region of the ferritin messenger RNA.  Previous studies have confirmed the binding of IRP to the ferritin IRE at the apical loop and bulge regions.  Our goal was to monitor the structural transitions of IRE as a function of IRP in greater detail.  In this project, Selective 2’ Hydroxyl Acylation analyzed by Primer Extension (SHAPE) chemistry was used to interrogate IRP binding-induced conformational changes in the ferritin IRE RNA.  It was found that nucleotides in the IRE bulge region preferentially interact with the IRP.  With the addition of more IRP to the RNA solution, there is a gradual decrease in the SHAPE reactivities of nucleotides in the apical loop of the IRE, indicating an increase in binding between IRP and the RNA loop.  <br/>

Investigation of the interactions between IRP and ferritin IRE

255th National Meeting (2018)

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