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Bioscience, Biotechnology, and Biochemistry Volume 70, 2006 - Issue 7
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Original Articles

A New Double-Stranded RNA Binding Protein (DRBP-120) Is Associated with Double-Stranded RNA-Activated Protein Kinase (PKR)

Shuji WATANABEDepartment of Physiology, School of Medicine, Iwate Medical University
,
Tetsuro YAMASHITADepartment of Agro-Bioscience, Faculty of Agriculture, Iwate University
&
Hideharu TAIRADepartment of Agro-Bioscience, Faculty of Agriculture, Iwate University
Pages 1717-1723 | Received 02 Feb 2006, Accepted 22 Mar 2006, Published online: 22 May 2014

  • 1) Samuel, C. E., Antiviral actions of interferon interferon-regulated cellular proteins and their surprisingly selective antiviral activities. Virology, 183, 1–11 (1991).
  • 2) Samuel, C. E., The eIF-2 alpha protein kinases, regulators of translation in eukaryotes from yeasts to humans. J. Biol. Chem., 268, 7603–7606 (1993).
  • 3) Mathews, M. B., and Shenk, T., Adenovirus virus-associated RNA and translation control. J. Virol., 65, 5657–5662 (1991).
  • 4) Park, H., Davies, M. V., Langland, J. O., Chang, H. W., Nam, Y. S., Tartaglia, J., Paoletti, E., Jacobs, B. L., Kaufman, R. J., and Venkatesan, S., TAR RNA-binding protein is an inhibitor of the interferon-induced protein kinase PKR. Proc. Natl. Acad. Sci. USA, 91, 4713–4717 (1994).
  • 5) Chang, H. W., Watson, J. C., and Jacobs, B. L., The E3L gene of vaccinia virus encodes an inhibitor of the interferon-induced, double-stranded RNA-dependent protein kinase. Proc. Natl. Acad. Sci. USA, 89, 4825–4829 (1992).
  • 6) Davies, M. V., Chang, H. W., Jacobs, B. L., and Kaufman, R. J., The E3L and K3L vaccinia virus gene products stimulate translation through inhibition of the double-stranded RNA-dependent protein kinase by different mechanisms. J. Virol., 67, 1688–1692 (1993).
  • 7) Lu, Y., Wambach, M., Katze, M. G., and Krug, R. M., Binding of the influenza virus NS1 protein to double-stranded RNA inhibits the activation of the protein kinase that phosphorylates the elF-2 translation initiation factor. Virology, 214, 222–228 (1995).
  • 8) Tan, S. L., Gale, M. J., Jr., and Katze, M. G., Double-stranded RNA-independent dimerization of interferon-induced protein kinase PKR and inhibition of dimerization by the cellular P58IPK inhibitor. Mol. Cell. Biol., 18, 2431–2443 (1998).
  • 9) Der, S. D., Yang, Y. L., Weissmann, C., and Williams, B. R., A double-stranded RNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis. Proc. Natl. Acad. Sci. USA, 94, 3279–3283 (1997).
  • 10) Meurs, E. F., Galabru, J., Barber, G. N., Katze, M. G., and Hovanessian, A. G., Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase. Proc. Natl. Acad. Sci. USA, 90, 232–236 (1993).
  • 11) Chong, K. L., Feng, L., Schappert, K., Meurs, E., Donahue, T. F., Friesen, J. D., Hovanessian, A. G., and Williams, B. R., Human p68 kinase exhibits growth suppression in yeast and homology to the translational regulator GCN2. EMBO J., 11, 1553–1562 (1992).
  • 12) Raveh, T., Hovanessian, A. G., Meurs, E. F., Sonenberg, N., and Kimchi, A., Double-stranded RNA-dependent protein kinase mediates c-Myc suppression induced by type I interferons. J. Biol. Chem., 271, 25479–25484 (1996).
  • 13) Osman, F., Jarrous, N., Ben-Asouli, Y., and Kaempfer, R., A cis-acting element in the 3′-untranslated region of human TNF-alpha mRNA renders splicing dependent on the activation of protein kinase PKR. Genes Dev., 13, 3280–3293 (1999).
  • 14) Benkirane, M., Neuveut, C., Chun, R. F., Smith, S. M., Samuel, C. E., Gatignol, A., and Jeang, K. T., Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR. EMBO J., 16, 611–624 (1997).
  • 15) Saunders, L. R., Perkins, D. J., Balachandran, S., Michaels, R., Ford, R., Mayeda, A., and Barber, G. N., 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., 276, 32300–32312 (2001).
  • 16) Kumar, K. U., Srivastava, S. P., and Kaufman, R. J., Double-stranded RNA-activated protein kinase (PKR) is negatively regulated by 60S ribosomal subunit protein L18. Mol. Cell. Biol., 19, 1116–1125 (1999).
  • 17) Yin, Z., Haynie, J., Williams, B. R., and Yang, Y. C., C114 is a novel IL-11-inducible nuclear double-stranded RNA-binding protein that inhibits protein kinase R. J. Biol. Chem., 278, 22838–22845 (2003).
  • 18) Gale, M., Jr., Blakely, C. M., Hopkins, D. A., Melville, M. W., Wambach, M., Romano, P. R., and Katze, M. G., Regulation of interferon-induced protein kinase PKR: modulation of P58IPK inhibitory function by a novel protein, P52rIPK. Mol. Cell. Biol., 18, 859–871 (1998).
  • 19) Melville, M. W., Tan, S. L., Wambach, M., Song, J., Morimoto, R. I., and Katze, M. G., The cellular inhibitor of the PKR protein kinase, P58(IPK), is an influenza virus-activated co-chaperone that modulates heat shock protein 70 activity. J. Biol. Chem., 274, 3797–3803 (1999).
  • 20) Patel, R. C., and Sen, G. C., PACT, a protein activator of the interferon-induced protein kinase, PKR. EMBO J., 17, 4379–4390 (1998).
  • 21) Ito, T., Yang, M., and May, W. S., RAX, a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. J. Biol. Chem., 274, 15427–15432 (1999).
  • 22) Jeffrey, I. W., Kadereit, S., Meurs, E. F., Metzger, T., Bachmann, M., Schwemmle, M., Hovanessian, A. G., and Clemens, M. J., Nuclear localization of the interferon-inducible protein kinase PKR in human cells and transfected mouse cells. Exp. Cell Res., 218, 17–27 (1995).
  • 23) Segawa, H., Kato, M., Yamashita, T., and Taira, H., The roles of individual cysteine residues of Sendai virus fusion protein in intracellular transport. J. Biochem., 123, 1064–1072 (1998).
  • 24) Galabru, J., and Hovanessian, A., Autophosphorylation of the protein kinase dependent on double-stranded RNA. J. Biol. Chem., 262, 15538–15544 (1987).
  • 25) Patel, R. C., Vestal, D. J., Xu, Z., Bandyopadhyay, S., Guo, W., Erme, S. M., Williams, B. R., and Sen, G. C., DRBP76, a double-stranded RNA-binding nuclear protein, is phosphorylated by the interferon-induced protein kinase, PKR. J. Biol. Chem., 274, 20432–20437 (1999).
  • 26) Parker, L. M., Fierro-Monti, I., and Mathews, M. B., Nuclear factor 90 is a substrate and regulator of the eukaryotic initiation factor 2 kinase double-stranded RNA-activated protein kinase. J. Biol. Chem., 276, 32522–32530 (2001).
  • 27) Patterson, J. B., and Samuel, C. E., Expression and regulation by interferon of a double-stranded-RNA-specific adenosine deaminase from human cells: evidence for two forms of the deaminase. Mol. Cell. Biol., 15, 5376–5388 (1995).
  • 28) Williams, B. R., PKR; a sentinel kinase for cellular stress. Oncogene, 18, 6112–6120 (1999).
  • 29) Bergeron, J., Benlimame, N., Zeng-Rong, N., Xiao, D., Scrivens, P. J., Koromilas, A. E., and Alaoui-Jamali, M. A., Identification of the interferon-inducible double-stranded RNA-dependent protein kinase as a regulator of cellular response to bulky adducts. Cancer Res., 60, 6800–6804 (2000).
  • 30) Takizawa, T., Tatematsu, C., Watanabe, M., Yoshida, M., and Nakajima, K., Three leucine-rich sequences and the N-terminal region of double-stranded RNA-activated protein kinase (PKR) are responsible for its cytoplasmic localization. J. Biochem., 128, 471–476 (2000).
  • 31) O’Farrell, P. Z., Goodman, H. M., and O’Farrell, P. H., High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell, 12, 1133–1141 (1977).

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