Nucleic Acids Research, Vol 25, Issue 13 2672-2678, Copyright © 1997 by Oxford University Press
RA Petryshyn, AG Ferrenz and J Li
PKR is a doubled-stranded RNA-dependent protein kinase which is implicated
in the regulation of several cellular processes, including cell
proliferation. PKR undergoes phosphorylation and activation in mouse
embryonic 3T3-F442A cells in response to endogenous RNA(s). Activation of
PKR is related to growth and differentiation of these cells. A cellular
regulatory RNA (R-RNA) which activates PKR has been isolated from these
cells and its cDNA partially sequenced. Here we have characterized the
R-RNA transcript with respect to nuclease sensitivity and the extent of
double-stranded structure involved in activation of PKR. The location of
the activating sequence was mapped to a contiguous 226/252 nt region of the
R-RNA transcript by hybridization to its cDNA fragments. Hybridization with
a panel of short oligodeoxynucleotides complementary to the R-RNA, coupled
with protein kinase analysis, was used to probe the 252 nt region for
critical sequences. Three short non-contiguous sequences which appear most
important for activation of PKR were identified within the 252 nt region.
Thus, these studies have identified specific sequences most important for
activation of PKR. Furthermore, since the above antisense
oligodeoxynucleotides inhibit enzyme activation, our results exemplify an
unusual mode of action of antisense sequences on the activation of PKR by
disruption of RNA secondary structure.
ARTICLES
Characterization and mapping of the double-stranded regions involved in activation of PKR within a cellular RNA from 3T3-F442A cells
Center for Cancer and Transplantation Biology, Children's National Medical Center, Washington, DC 20010, USA.
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  S. Solomon, Y. Xu, B. Wang, M. D. David, P. Schubert, D. Kennedy, and J. W. Schrader Distinct Structural Features ofCaprin-1 Mediate Its Interaction with G3BP-1 and Its Induction of Phosphorylation of Eukaryotic Translation Initiation Factor 2{alpha}, Entry to Cytoplasmic Stress Granules, and Selective Interaction with a Subset of mRNAs Mol. Cell. Biol., March 15, 2007; 27(6): 2324 - 2342. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. M. Nussbaum, S. Gunnery, and M. B. Mathews The 3'-untranslated regions of cytoskeletal muscle mRNAs inhibit translation by activating the double-stranded RNA-dependent protein kinase PKR Nucleic Acids Res., March 1, 2002; 30(5): 1205 - 1212. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 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]
|
|
|
|
 |
|
 M. Gale Jr., S.-L. Tan, and M. G. Katze Translational Control of Viral Gene Expression in Eukaryotes Microbiol. Mol. Biol. Rev., June 1, 2000; 64(2): 239 - 280. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. A. Vickers, J. R. Wyatt, and S. M. Freier Effects of RNA secondary structure on cellular antisense activity Nucleic Acids Res., March 15, 2000; 28(6): 1340 - 1347. [Abstract] [Full Text] [PDF]
|
|