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J Biol Chem, Vol. 273, Issue 37, 23637-23640, September 11, 1998
,
From the A family of noncoding mRNA sequences,
iron-responsive elements (IREs), coordinately regulate several
mRNAs through binding a family of mRNA-specific proteins, iron
regulatory proteins (IRPs). IREs are hairpins with a constant terminal
loop and base-paired stems interrupted by an internal loop/bulge (in
ferritin mRNA) or a C-bulge (in m-aconitase, erythroid
aminolevulinate synthase, and transferrin receptor mRNAs). IRP2
binding requires the conserved C-G base pair in the terminal loop,
whereas IRP1 binding occurs with the C-G or engineered U-A. Here we
show the contribution of the IRE internal loop/bulge to IRP2 binding by
comparing natural and engineered IRE variants. Conversion of the
internal loop/bulge in the ferritin-IRE to a C-bulge, by deletion of U,
decreased IRP2 binding by >95%, whereas IRP1 binding changed only
13%. Moreover, IRP2 binding to natural IREs with the C-bulge was
similar to the Department of Biochemistry, North Carolina
State University, Raleigh, North Carolina 27695-7622, the
§ Department of Medicine and the Eccles Program in Human
Molecular Biology and Genetics, University of Utah, Salt Lake City,
Utah 84112, and the ¶ Department of Microbiology and Immunology,
University of Illinois, Chicago, Illinois 60612
U6 ferritin-IRE: >90% lower than the
ferritin-IRE. The results predict mRNA-specific variation in
IRE-dependent regulation in vivo and may relate
to previously observed differences in iron-induced ferritin and
m-aconitase synthesis in liver and cultured cells. Variations in IRE
structure and cellular IRP1/IRP2 ratios can provide a range of finely
tuned, mRNA-specific responses to the same (iron) signal.
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