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Papers In Press, published online ahead of print November 19, 2001
CHORI, (Children's Hospital Oakland Research Institute), Oakland, CA 94609
Corresponding Author: etheil{at}chori.org
Messenger RNA (mRNA) regulatory elements often form helices specifically distorted by loops or bulges, which control protein synthesis rates in vitro. Do such three-dimensional RNA structures form in vivo? We now observe formation of the internal loop/bulge (IL/B structure) in the IRE (Iron Responsive Element) of ferritin mRNA expressed in HeLa cells, using radical cleavage with Cu-phen (Cu-1,10-phenantholine), and protection of the loop/bulge by the regulatory protein (IRP), expressed by cotransfection. Cu-phen, a metal complex (MC) selected because of binding and cleavage at the IL/B in solution, recognized the same site in mRNA in HeLa cells. Endogenous reductants apparently substituted for the sulfhydryl activation of Cu-phen cleavage in solution. Selective RNA IL/B recognition by Cu-phen in vivo is emphasized by resistance to cleavage of a mutated, IL/B IRE in ferritin mRNA. Development of small MCs even more selective than Cu-phen can exploit three-dimensional mRNA or viral RNA structures in vivo to manipulate RNA function. Formation in vivo of the IL/B in the ferritin IRE, which is associated in vitro with greater repression than single IRE structures in other mRNAs, likely contributes to larger derepression of ferritin synthesis in vivo triggered by signals for the IRE/IRP system.
J. Biol. Chem, 10.1074/jbc.C100614200
Submitted on October 24, 2001
Revised on November 19, 2001
Accepted on November 19, 2001
An mRNA loop/bulge in the ferritin iron responsive element (IRE) formed in vivo, and detected by radical probing with Cu-phen and protein (IRP) footprinting
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