Nucleic Acids Research, Vol 25, Issue 16 3362-3370, Copyright © 1997 by Oxford University Press
ZE Zehner, RK Shepherd, J Gabryszuk, TF Fu, M Al-Ali and WM Holmes
Several functions have been attributed to protein binding within the
3'untranslated region (3'UTR) of mRNA, including mRNA localization,
stability, and translational repression. Vimentin is an intermediate
filament protein whose 3'untranslated sequence is highly conserved between
species. In order to identify sequences that might play a role in vimentin
mRNA function, we synthesized32P-labeled RNA from different regions of
vimentin's 3'UTR and assayed for protein binding with HeLa extracts using
band shift assays. Sequences required for binding are contained within a
region 61-114 nucleotides downstream of the stop codon, a region which is
highly conserved from Xenopus to man. As judged by competition assays,
binding is specific. Solution probing studies of 32P-labeled RNA with
various nucleases and lead support a complex stem and loop structure for
this region. Finally, UV cross- linking of the RNA-protein complex
identifies an RNA binding protein of 46 kDa. Fractionation of a HeLa
extract on a sizing column suggests that in addition to the 46 kDa protein,
larger complexes containing additional protein(s) can be identified.
Vimentin mRNA has been shown to be localized to the perinuclear region of
the cytoplasm, possibly at sites of intermediate filament assembly. To
date, all sequences required for localization of various mRNAs have been
confined to the 3'UTR. Therefore, we hypothesize that this region and
associated protein(s) might be important for vimentin mRNA function such as
in localization.
ARTICLES
RNA-protein interactions within the 3 ' untranslated region of vimentin mRNA
Department of Biochemistry and Molecular Biophysics, Box 980614, Medical College of Virginia, Virginia Commonwealth University, Richmond, VA 23298-0614, USA. zehner@gems.vcu.edu
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