Developmental regulation of a plant encoded inhibitor of eukaryotic initiation factor 2α phosphorylation

Plant Journal

Volumn 12, Issue 2, 1997, Pages 393-400

  Langland, Jeffrey O ^a,b   Langland, Lisa ^a   Zeman, Cameron ^b   Saha, Debabrata ^c   Roth, Don A ^a  

^a UNIVERSITY OF WYOMING   (United States)

^b ARIZONA STATE UNIVERSITY   (United States)

^c UNIVERSITY OF NEBRASKA LINCOLN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR 2; MONOCLONAL ANTIBODY; PROTEIN KINASE R; PROTEIN SERINE THREONINE KINASE; VEGETABLE PROTEIN;

ARTICLE; BIOSYNTHESIS; CROSS REACTION; DRUG ANTAGONISM; GENE EXPRESSION REGULATION; GLYCOSYLATION; HUMAN; ISOLATION AND PURIFICATION; METABOLISM; PHOSPHORYLATION; PLANT LEAF; RETICULOCYTE;

ANTIBODIES, MONOCLONAL; CROSS REACTIONS; EIF-2 KINASE; EUKARYOTIC INITIATION FACTOR-2; GENE EXPRESSION REGULATION, DEVELOPMENTAL; GENE EXPRESSION REGULATION, PLANT; GLYCOSYLATION; HUMANS; PHOSPHORYLATION; PLANT LEAVES; PLANT PROTEINS; PROTEIN-SERINE-THREONINE KINASES; RETICULOCYTES;

EUKARYOTA; TRITICUM AESTIVUM;

EID: 0031213922     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-313X.1997.12020393.x     Document Type: Article

References (42)

1. Arfin, S.M., Kendall, R.L., Hall, L., Weaver, L.H., Stewart, A.E., Matthews, B.W. and Bradshaw, R.A. (1995) Eukaryotic methionyl aminopeptidases: Two classes of cobalt-dependent enzymes. Proc. Natl Acad. Sci. USA, 92, 7714-7718.
2. Bazan, J.F., Weaver, L.H., Roderick, S.L., Huber, R. and Matthews, B.W. (1994) Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold. Proc. Natl Acad. Sci. USA, 91, 2473-2477.
3. Carroll, K., Elroy-Stein, O., Moss, B. and Jagus, R. (1993) Recombinant vaccinia virus K3L gene product prevents activation of double-stranded RNA-dependent, initiation factor 2a-specific protein kinase. J. Biol. Chem. 268, 12 837-12 842.
4. Chakraborty, A., Saha, D., Bose, A., Chatterjee, M. and Gupta, N.K, (1994a) Regulation of elF-2α-subunit phosphorylation in reticulocyte lysate. Biochemistry, 33, 6700-6706.
5. Chakraborty, A., Saha, D., Bose, A., Hileman, R.E., Chatterjee, M. and Gupta, N.K. (1994b) Mechanism of action of an eukaryotic initiation factor-2 (elF-2) associated 67 kDa glycoprotein (p67) and an elF-2 kinase (dsl). Indian J. Biochem. Biophys. 31, 236-242.
6. Chang, H.W., Watson, J.C. and Jacobs, B.L. (1992) 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.
7. Chen, J.-J. and London, I.M. (1995) Regulation of protein synthesis by heme-regulated elF-2α kinase. Trends Biochem. Sci. 20, 105-108.
8. Chong, K.L., Feng, L., Schappert, K., Meurs, E., Donahue, T.F., Friesen, J.D., Hovanessian, A.G. and Williams, B.R.G. (1992) Human p68 kinase exhibits growth suppression in yeast and homology to the translations! regulator GCN2. EMBO J. 11, 1653-1562.
9. Chu, N.M., Janckila, A.J., Wallace, J.H. and Yam, L.T. (1989) Assessment of a method for immunochemical detection of antigens on nitrocellulose membranes. J. Histochem. Cytochem. 37, 257-263.
10. Clemens, M. (1992) Suppression with a difference. Nature 360, 210-211.
11. Clemens, M. (1996) Protein kinases that phosphorylate elF2 and elF2B, and their role in eukaryotic cell translational control. Translational Control (Hershey, J.W.B., Mathews, M. B. and Sonenberg, N., eds). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
12. Crum, C.J., Hiddinga, H.J. and Roth, D.A. (1988) Tobacco mosaic virus infection stimulates the phosphorylation of a plant protein associated with double-stranded RNA-dependent protein kinase activity. J. Biol. Chem, 263, 13 440-13 443.
13. Cuming, A.C. and Lane, E.G. (1979) Protein synthesis in imbibing wheat embryos. Eur. J. Biochem. 99, 217-224.
14. Datta, B., Chakrabarti, D., Roy, A. and Gupta, N.K. (1988) Roles of a 67-kDa polypeptide in reversal of protein synthesis inhibition in heme-deficient reticulocyte lysate. Proc. Natl Acad. Sci. USA, 85, 3324-3328.
15. Datta, B., Ray, M.K., Chakrabarti, D., Wylie, D.E. and Gupta, N.K. (1989) Glycosylation of eukaryotic peptide chain initiation factor 2 (elF-2)-associated 67-kDa polypeptide (p67) and its possible role in the inhibition of elF-2 kinase-catalyzed phosphorylation of the elF-2α-subunit. J. Biol. Chem. 264, 20 620-20 624.
16. DeBenedetti, A. and Baglioni, C. (1984) Inhibition of mRNA binding to ribosomes by localized activation of dsRNA-dependent protein kinase. Nature, 311, 79-81.
17. De Jimenez, E.S. and Aguilar, R. (1984) Protein synthesis patterns: relevance of old and new messenger RNA in germinating maize embryos. Plant Physiol. 75, 231-234.
18. Dever, T.E., Feng, L., Wek, R.C., Cigan, A.M., Donahue, T.F. and Hinnebusch, A.G. (1992) Phosphorylation of initiation factor 2a by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast. Cell, 68, 585-596.
19. Dubois, M.F., Galabru, J., Lebon, P., Safer, B. and Hovanessian, A.G. (1989) Reduced activity of the Interferon induced double-stranded RNA-dependent protein kinase during a heat shock stress. J. Biol. Chem. 264, 12 165-12 171.
20. Gupta, S., Wu, S., Chatterjee, N., IIan, J., IIan, J., Osterman, J.C. and Gupta, N.K. (1995) Regulation of an eukaryotic initiation factor-2 (elF-2) associated 67 kDa glycoprotein (p67) and its requirement in protein synthesis. Gene Expression, 5, 113-122.
21. Hart, G.W., Holt, G.D. and Hattiwanger, R.S. (1988) Nuclear and cytoplasmic glycosylation: novel saccharide linkages in unexpected places. Trends Biochem. Sci. 13, 380-384.
22. Hiddinga, H.J., Crum, C.J. and Roth, D.A. (1988) Viroid-induced phosphorylation of a host protein related to a dsRNA-dependent protein kinase. Science, 241, 451-453.
23. Hovanessian, A.G. (1989) The double-stranded RNA-activated protein kinase induced by interferon: dsRNA-PK. J. Interferon Hes. 9, 641-647.
24. Hovanessian, A.G. and Galabru, J. (1987) The double-stranded RNA-dependent protein kinase is also activated by heparin. Eur. J. Biochem. 167, 467-473.
25. Hu, J. and Roth, D.A. (1991) Temporal regulation of tobacco mosaic virus-induced phosphorylation of a host encoded protein. Biochem. Biophys. Res. Commun. 179, 229-235.
26. Johnston, F.B. and Stern, H. (1957) Mass isolation of viable wheat embryos. Nature, 175, 160-161.
27. Katze, M.G. (1992) The war against the interferon-induced dsRNA activated protein kinase: can viruses win? J. Interferon Res. 12, 241-248.
28. Kaufmann, R.J., Davies, M.V., Pathak, V.K. and Hershey, J.W.B. (1989) The phosphorylation state of eukaryotic initiation factor 2 alters translational efficiency of specific mRNAs. Mol. Cell Biol. 9, 946-958.
29. Koromilas, A.E., Roy, S., Barber, G.N., Katze, M.G. and Sonenberg, N. (1992) Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase. Science, 257, 1685-1689.
30. Langland, J.O., Song, J., Jacobs, B. and Roth, D.A. (1995) Identification of a plant-encoded analog of PKR, the mammalian double-strandad RNA-dependent protein kinase. Plant Physiol. 108, 1259-1267.
31. Langland, J.O., Langland, L.A., Browning, K.S. and Roth, D.A. (1996a) Phosphorylation of plant eukaryotic initiation factor-2 by the plant encoded double-stranded RNA-dependent protein kinase, pPKR, and inhibition of protein synthesis in vitro. J. Biol. Chem. 271, 4539-4544.
32. Langland, J.O., Langland, L.A. and Roth, D.A. (1996b) Polyanion regulation of the plant-encoded double-stranded RNA-dependent protein kinase (pPKR,). Plant Physiol. Biochem. 34, 521-526.
33. Lee, S.B. and Esteban, M. (1994). The interferon-induced double-stranded RNA-activated protein kinase induces apoptosis. Virology, 199, 491-496.
34. Merrick, W.C. and Hershey, J.W.B. (1996) The pathway and mechanism of eukaryotic protein synthesis. Translational Control (Hershey, J.W.B., Mathews, M. B. and Sonenberg, N., eds). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
35. Meurs, E., Galabru, J., Barber, G.N., Katze, M.G. and Hovanessian, A.G. (1993) Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase. Proc. Natl Acad. Sci. USA, 90, 232-236.
36. Ray, M.K., Datta, B., Chakraborty, A., Chattopadhyay, A., Meza-Keuthen, S. and Gupta, N.K. (1992) The eukaryotic initiation factor 2-associated 67-kDa polypeptide (p67) plays a critical role in regulation of protein synthesis initiation in animal cells. Proc. Natl Acad, Sci. USA, 89, 539-543.
37. Roth, D.A. and He, X. (1994) Viral dependent phosphorylation of a dsRNA-dependent kinase. Prog. Mol. Subcell. Biol. 14, 28-47.
38. Samuel, C.E. (1991) Antiviral actions of interferon-regulated cellular proteins and their surprisingly selective antiviral activities. Virology, 183, 1-11.
39. Samuel, C.E. (1993) The elF-2α protein kinases, regulators of translation in eukaryotes from yeasts to humans. J. Biol. Chem. 268, 7603-7606.
40. St. Johnston, A., Brown, N.H., Gall, J.G. and Jantsch, M. (1992) A conserved double-stranded RNA-binding domain. Proc. Natl Acad. Sci. USA, 89, 10 979-10 983.
41. Trachsel, H. (1996) Binding of initiator methionyl-tRNA to ribosomes. Translational Control (Hershey, J.W.B., Mathews, M.B. and Sonenberg, N., eds). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
42. Wu, S., Gupta, S., Chatterjee, N., Hileman, R.E., Kinzy, T.G., Denslow, N. D., Merrick, W. C., Chakrabarti, D., Osterman, J.C. and Gupta, N.K. (1993) Cloning and characterization of complementary DMA encoding the eukaryotic initiation factor 2-associated 67-kDa protein (p67). J. Biol. Chem. 268, 10 796-10 801.