The 5′-Untranslated Region of Human Transferrin mRNA, Which Contains a Putative Iron-Regulatory Element, Is Bound by Purified Iron-Regulatory Protein in a Sequence-Specific Manner

Laura A. Cox, Mary Claire Kennedy, Gwendolyn S. Adrian

    Research output: Contribution to journalArticlepeer-review

    18 Scopus citations

    Abstract

    Human transferrin mRNA contains a 5′-untranslated region that (1) has homology to an iron responsive element and (2) is implicated in translational iron regulation of human transferrin transgenes in transgenic mice. Ferritin mRNA contains a 5′-untranslated region iron-responsive element, but iron regulation of ferritin differs from that of human transferrin transgenes in both magnitude and direction. Structural differences between the ferritin iron-responsive element and the human transferrin putative iron-responsive element may influence their iron-regulatory protein interactions and direct the differing translational responses. This study examines human transferrin RNA nucleotide sequence requirements for binding of cytoplasmic proteins and purified iron-regulatory protein. Mutations of the putative transferrin iron-responsive element similarly affected binding of purified iron-regulatory protein and liver cytoplasmic proteins, providing evidence that the IRP is one of the liver cytoplasmic proteins that binds the human transferrin iron-regulatory element and suggesting that it may be involved in iron-regulation of transferrin.

    Original languageEnglish (US)
    Pages (from-to)925-932
    Number of pages8
    JournalBiochemical and Biophysical Research Communications
    Volume212
    Issue number3
    DOIs
    StatePublished - Jan 1 1995

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Cell Biology

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