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J Biol Chem, Vol. 274, Issue 36, 25447-25454, September 3, 1999
From the Department of Cell Biology, Lerner Research Institute,
Cleveland Clinic Foundation, Cleveland, Ohio 44195
In mammalian selenoprotein mRNAs, the highly
structured 3' UTR contains selenocysteine insertion sequence (SECIS)
elements that are required for the recognition of UGA as the
selenocysteine codon. Our previous work demonstrated a tight
correlation between codon-specific translational read-through and the
activity of a 120-kDa RNA-binding protein that interacted specifically
with the SECIS element in the phospholipid hydroperoxide glutathione peroxidase mRNA. This study reports the RNA binding and biochemical properties of this protein, SECIS-binding protein 2 (SBP2). We detected
SBP2 binding activity in liver, hepatoma cell, and testis extracts from
which SBP2 has been purified by anion exchange and RNA affinity
chromatography. This scheme has allowed us to identify a 120-kDa
polypeptide that co-elutes with SBP2 binding activity from wild-type
but not mutant RNA affinity columns. A characterization of SBP2
biochemical properties reveals that SBP2 binding is sensitive to
oxidation and the presence of heparin, rRNA, and poly(G). SBP2 activity
elutes with a molecular mass of ~500 kDa during gel filtration chromatography, suggesting the existence of a large functional complex.
Direct cross-linking and competition experiments demonstrate that the
minimal phospholipid hydroperoxide glutathione peroxidase 3' UTR
binding site is between 82 and 102 nucleotides, which correlates with
the minimal sequence necessary for translational read-through. SBP2
also interacts specifically with the minimally functional 3' UTR of
another selenoprotein mRNA, deiodinase 1.
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