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Nucleic Acids Research 2005 33(14):4507-4518; doi:10.1093/nar/gki763
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Published online 9 August 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

Novel DNA-binding properties of the RNA-binding protein TIAR

Esther A. Suswam1,3, Yan Yan Li1,3, Harry Mahtani1,3 and Peter H. King1,2,3,*

1Department of Neurology, University of Alabama Birmingham, AL 35295, USA 2Department of Physiology and Biophysics, University of Alabama Birmingham, AL 35295, USA 3Birmingham Veterans Affairs Medical Center Birmingham, AL 35295, USA

*To whom correspondence should be addressed. Tel: +1 205 975 8116; Fax: +1 205 934 0928; Email: pking{at}uab.edu

Received May 20, 2005. Revised July 6, 2005. Accepted July 25, 2005.

TIA-1 related protein binds avidly to uridine-rich elements in mRNA and pre-mRNAs of a wide range of genes, including interleukin (IL)-8 and vascular endothelial growth factor (VEGF). The protein has diverse regulatory roles, which in part depend on the locus of binding within the transcript, including translational control, splicing and apoptosis. Here, we observed selective and potent inhibition of TIAR–RNP complex formation with IL-8 and VEGF 3'-untranslated regions (3'-UTRs) using thymidine-rich deoxyoligonucleotide (ODN) sequences derived from the VEFG 3'-UTR. We show by ultraviolet crosslinking and electrophoretic mobility shift assays that TIAR can bind directly to single-stranded, thymidine-rich ODNs but not to double-stranded ODNs containing the same sequence. TIAR had a nearly 6-fold greater affinity for DNA than RNA ( versus 9.4 x 10–9 M). Truncation of TIAR indicated that the high affinity DNA-binding site overlaps with the RNA-binding site involving RNA recognition motif 2 (RRM2). However, RRM1 alone could also bind to DNA. Finally, we show that TIAR can be displaced from single-stranded DNA by active transcription through the binding site. These results provide a potential mechanism by which TIAR can shuttle between RNA and DNA ligands.


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