Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (780K) 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 (14)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Coolidge, C. J.
Right arrow Articles by Patton, J. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Coolidge, C. J.
Right arrow Articles by Patton, J. G.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2000, Vol. 28, No. 6 1407-1417
© 2000 Oxford University Press

A new double-stranded RNA-binding protein that interacts with PKR

Candace J. Coolidge and James G. Patton*

Department of Molecular Biology, Box 1820, Station B, Vanderbilt University, Nashville, TN 37235, USA

We have identified a 74 kDa double-stranded (ds)RNA-binding protein that shares extensive homology with the mouse spermatid perinuclear RNA-binding (Spnr) protein. p74 contains two dsRNA-binding motifs (dsRBMs) that are essential for preferential binding to dsRNA. Previously, dsRNA-binding proteins were shown to undergo homo- and heterodimerization, raising the possibility that regulation of activity could be controlled by interactions between different family members. Homodimerization is required to activate the dsRNA-dependent protein kinase PKR, whereas hetero­dimerization between PKR and other dsRNA-binding proteins can inhibit kinase activity. We have found that p74 also interacts with PKR, both the wild-type enzyme and a catalytically defective mutant (K296R). While co-expression of p74 and wild-type PKR in the yeast Saccharomyces cerevisiae did not alter PKR activity, co-expression of p74 and the catalytically defective K296R mutant surprisingly resulted in abnormal morphology and cell death in transformants that maintained a high level of p74 expression. These transformants could be rescued by overexpression of the {alpha}-subunit of wild-type eukaryotic translation initiation factor 2 (eIF2{alpha}), one of the known substrates for PKR. We hypothesize that competing heterodimers between p74–K296R PKR and eIF2{alpha}–K296R PKR may control cell growth such that stabilization of the p74–K296R PKR heterodimer induces abnormal morphology and cell death.

* To whom correspondence should be addressed. Tel: +1 615 322 4738; Fax: +1 615 343 6707; Email: james.g.patton@vanderbilt.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
 J. Biol. Chem.Home page
G. P. Scarlett, S. J. Elgar, P. D. Cary, A. M. Noble, R. L. Orford, G. G. Kneale, and M. J. Guille
Intact RNA-binding Domains Are Necessary for Structure-specific DNA Binding and Transcription Control by CBTF122 during Xenopus Development
J. Biol. Chem., December 10, 2004; 279(50): 52447 - 52455.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Z. Yin, J. Haynie, B. R. G. Williams, and Y.-C. Yang
C114 Is a Novel IL-11-inducible Nuclear Double-stranded RNA-binding Protein That Inhibits Protein Kinase R
J. Biol. Chem., June 13, 2003; 278(25): 22838 - 22845.
[Abstract] [Full Text] [PDF]

Home page
 FASEB J.Home page
L. R. SAUNDERS and G. N. BARBER
The dsRNA binding protein family: critical roles, diverse cellular functions
FASEB J, June 1, 2003; 17(9): 961 - 983.
[Abstract] [Full Text] [PDF]

Home page
 RNAHome page
T. W. REICHMAN and M. B. MATHEWS
RNA binding and intramolecular interactions modulate the regulation of gene expression by nuclear factor 110
RNA, May 1, 2003; 9(5): 543 - 554.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
T. W. Reichman, L. C. Muniz, and M. B. Mathews
The RNA Binding Protein Nuclear Factor 90 Functions as Both a Positive and Negative Regulator of Gene Expression in Mammalian Cells
Mol. Cell. Biol., January 1, 2002; 22(1): 343 - 356.
[Abstract] [Full Text] [PDF]

Home page
 Cold Spring Harb Symp Quant BiolHome page
L.M. PARKER, I. FIERRO-MONTI, T.W. REICHMAN, S. GUNNERY, and M.B. MATHEWS
Double-stranded RNA-binding Proteins and the Control of Protein Synthesis and Cell Growth
Cold Spring Harb Symp Quant Biol, January 1, 2001; 66(0): 485 - 498.
[Abstract] [PDF]

Home page
 J. Biol. Chem.Home page
L. R. Saunders, D. J. Perkins, S. Balachandran, R. Michaels, R. Ford, A. Mayeda, and G. N. Barber
Characterization of Two Evolutionarily Conserved, Alternatively Spliced Nuclear Phosphoproteins, NFAR-1 and -2, That Function in mRNA Processing and Interact with the Double-stranded RNA-dependent Protein Kinase, PKR
J. Biol. Chem., August 17, 2001; 276(34): 32300 - 32312.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. M. Parker, I. Fierro-Monti, and M. B. Mathews
Nuclear Factor 90 Is a Substrate and Regulator of the Eukaryotic Initiation Factor 2 Kinase Double-stranded RNA-activated Protein Kinase
J. Biol. Chem., August 24, 2001; 276(35): 32522 - 32530.
[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.