Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (243K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (8)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Vuyisich, M.
Right arrow Articles by Beal, P. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vuyisich, M.
Right arrow Articles by Beal, P. A.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2000, Vol. 28, No. 12 2369-2374
© 2000 Oxford University Press

Regulation of the RNA-dependent protein kinase by triple helix formation

Momchilo Vuyisich and Peter A. Beal*

Department of Chemistry, University of Utah, Salt Lake City, UT 84112, USA

The RNA-dependent protein kinase (PKR) is an interferon-induced, RNA-activated enzyme that phos­phorylates the {alpha}-subunit of the translation initiation factor eIF-2, inhibiting its function. PKR is activated in vitro by binding to double-stranded RNA (dsRNA) molecules of ~30 bp or longer. Here we show that triple helix forming oligonucleotides (TFOs) inhibit dsRNA binding to the isolated RNA binding domain of PKR. The inhibition is specific to the targeted RNA and dependent on TFO length. Binding to a 30 bp duplex is inhibited by a 28 nt TFO and a 20 nt TFO with an IC50 of 35 ± 2 and 210 ± 22 nM, respectively. An 18 nt TFO partially inhibits binding. The activation of the kinase domain of PKR by a 30 bp RNA duplex is also inhibited by a 28 nt TFO. Inhibition of binding is most effective when the triple helix is formed prior to addition of the protein. These results indicate that triplex formation can be used to prevent the binding of an RNA binding protein with dsRNA-binding motifs.

* To whom correspondence should be addressed. Tel: +1 801 585 9719; Fax: +1 801 581 8433; Email: beal@chemistry.chem.utah.edu


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Nucleic Acids ResHome page
S. Ivanov, Y. Alekseev, J.-R. Bertrand, C. Malvy, and M. B. Gottikh
Formation of stable triplexes between purine RNA and pyrimidine oligodeoxyxylonucleotides
Nucleic Acids Res., July 15, 2003; 31(14): 4256 - 4263.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
N. V. Jammi and P. A. Beal
Phosphorylation of the RNA-dependent protein kinase regulates its RNA-binding activity
Nucleic Acids Res., July 15, 2001; 29(14): 3020 - 3029.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. Y. Yi-Brunozzi, O. M. Stephens, and P. A. Beal
Conformational Changes That Occur during an RNA-editing Adenosine Deamination Reaction
J. Biol. Chem., October 5, 2001; 276(41): 37827 - 37833.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.