Nucleic Acids Research, Vol 24, Issue 3 464-469, Copyright © 1996 by Oxford University Press
N Hubert, R Walczak, P Carbon and A Krol
Several gene products are involved in co-translational insertion of
selenocysteine by the tRNA(Sec). In addition, a stem-loop structure in the
mRNAs coding for selenoproteins is essential to mediate the selection of
the proper selenocysteine UGA codon. Interestingly, in eukaryotic
selenoprotein mRNAs, this stem-loop structure, the selenocysteine insertion
sequence (SECIS) element, resides in the 3'- untranslated region, far
downstream of the UGA codon. In view of unravelling the underlying complex
mechanism, we have attempted to detect RNA-binding proteins with
specificity for the SECIS element. Using mobility shift assays, we could
show that a protein, present in different types of mammalian cell extracts,
possesses the capacity of binding the SECIS element of the selenoprotein
glutathione peroxidase (GPx) mRNA. We have termed this protein SBP, for
Secis Binding Protein. Competition experiments attested that the binding is
highly specific and UV cross-linking indicated that the protein has an
apparent molecular weight in the range of 60-65 kDa. Finally, some data
suggest that the SECIS elements in the mRNAs of GPx and another
selenoprotein, type I iodothyronine 5' deiodinase, recognize the same SBP
protein. This constitutes the first report of the existence of a 3' UTR
binding protein possibly involved in the eukaryotic selenocysteine
insertion mechanism.
ARTICLES
A protein binds the selenocysteine insertion element in the 3'-UTR of mammalian selenoprotein mRNAs
UPR 9002 du CNRS, IBMC, Strasbourg, France.
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