Access the full text.
Sign up today, get DeepDyve free for 14 days.
Loading next page...
/lp/springer_journal/specific-in-vitro-phosphorylation-of-plant-eif2-by-eukaryotic-eif2-Ajt2GvAYim
References (41)
-
P. Mueller, Patrick Grueter, A. Hinnebusch, H. Trachsel (1998)
A Ribosomal Protein Is Required for Translational Regulation of GCN4 mRNAThe Journal of Biological Chemistry, 273
-
A. Hovanessian, J. Galabru (1987)
The double-stranded RNA-dependent protein kinase is also activated by heparin.European journal of biochemistry, 167 3
-
'. KarenL.Chong, Lan Feng, K. Schappert, E. Meurs, T. Donahue, '. JamesD.Friesen, A. Hovanessian, '. BryanR.G.Williams (1992)
Human p68 kinase exhibits growth suppression in yeast and homology to the translational regulator GCN2.The EMBO Journal, 11
-
J. Langland, Songmo Jin, B. Jacobs, D. Roth (1995)
Identification of a Plant-Encoded Analog of PKR, the Mammalian Double-Stranded RNA-Dependent Protein Kinase, 108
-
L. Manche, S. Green, C. Schmedt, M. Mathews (1992)
Interactions between double-stranded RNA regulators and the protein kinase DAIMolecular and Cellular Biology, 12
-
W. Merrick (1992)
Mechanism and regulation of eukaryotic protein synthesis.Microbiological reviews, 56 2
-
J. Hu, D. Roth (1991)
Temporal regulation of tobacco mosaic virus-induced phosphorylation of a host encoded protein.Biochemical and biophysical research communications, 179 1
-
Rekha Patel, G. Sen (1998)
PACT, a protein activator of the interferon‐induced protein kinase, PKRThe EMBO Journal, 17
-
(1998)
The translational machinery of plants -
Peter Kennelly, E. Krebs (1991)
Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases.The Journal of biological chemistry, 266 24
-
H. Trachsel (1996)
4 Binding of Initiator Methionyl-tRNA to RibosomesCold Spring Harbor Monograph Archive, 30
-
M. Clemens (1996)
5 Protein Kinases That Phosphorylate eIF2 and eIF2B, and Their Role in Eukaryotic Cell Translational ControlCold Spring Harbor Monograph Archive, 30
-
T. Dever, Lan Feng, R. Wek, A. Cigan, T. Donahue, A. Hinnebusch (1992)
Phosphorylation of initiation factor 2α by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeastCell, 68
-
J. Langland, L. Langland, K. Browning, D. Roth (1996)
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(*)The Journal of Biological Chemistry, 271
-
(1993)
The eIF2 -
C. Proud, D. Colthurst, S. Ferrari, L. Pinna (1991)
The substrate specificity of protein kinases which phosphorylate the alpha subunit of eukaryotic initiation factor 2.European journal of biochemistry, 195 3
-
J. Berlanga, S. Herrero, C. Haro (1998)
Characterization of the Hemin-sensitive Eukaryotic Initiation Factor 2α Kinase from Mouse Nonerythroid Cells*The Journal of Biological Chemistry, 273
-
G. Pavitt, K. Ramaiah, S. Kimball, A. Hinnebusch (1998)
eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange.Genes & development, 12 4
-
(1998)
Actvation of the dsRNA-dependent protein kinase, PKR, induces apoptosis through FADD-mediated death signalling -
C. Crum, J. Hu, H. Hiddinga, D. Roth (1988)
Tobacco mosaic virus infection stimulates the phosphorylation of a plant protein associated with double-stranded RNA-dependent protein kinase activity.The Journal of biological chemistry, 263 26
-
T. Dever, Jane-Jane Chen, G. Barber, A. Cigan, Lan Feng, T. Donahue, I. London, M. Katze, A. Hinnebusch (1993)
Mammalian eukaryotic initiation factor 2 alpha kinases functionally substitute for GCN2 protein kinase in the GCN4 translational control mechanism of yeast.Proceedings of the National Academy of Sciences of the United States of America, 90
-
Sang Lee, D. Rodríguez, J. Rodríguez, M. Esteban (1997)
The apoptosis pathway triggered by the interferon-induced protein kinase PKR requires the third basic domain, initiates upstream of Bcl-2, and involves ICE-like proteases.Virology, 231 1
-
(1997)
Cloning and characterization of a CDNA encoding a protein synthesis initiation factor2 α ( eIF 2 α ) kinase from Drosophila melanogaster -
J. Langland, L. Langland, D. Roth (1996)
Polyanion regulation of the plant-encoded double-stranded RNA-dependent protein kinase (pPKR)Plant Physiology and Biochemistry, 34
-
H. Hiddinga, C. Crum, J. Hu, D. Roth (1988)
Viroid-induced phosphorylation of a host protein related to a dsRNA-dependent protein kinase.Science, 241 4864
-
B. Kemp, R. Pearson (1990)
Protein kinase recognition sequence motifs.Trends in biochemical sciences, 15 9
-
J. Randal, Kaufman, V. Monique, Davies, '. Pathak, J. Hershey (1989)
The phosphorylation state of eucaryotic initiation factor 2 alters translational efficiency of specific mRNAsMolecular and Cellular Biology, 9
-
M. Kawagishi-Kobayashi, J. Silverman, Tekly Ung, T. Dever (1997)
Regulation of the protein kinase PKR by the vaccinia virus pseudosubstrate inhibitor K3L is dependent on residues conserved between the K3L protein and the PKR substrate eIF2alphaMolecular and Cellular Biology, 17
-
(1992)
Mutations activating the yeast eIF2 -
A. Hinnebusch (1996)
7 Translational Control of GCN4: Gene-specific Regulation by Phosphorylation of elF2Cold Spring Harbor Monograph Archive, 30
-
E. Meurs, J. Galabru, G. Barber, M. Katze, A. Hovanessian (1993)
Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase.Proceedings of the National Academy of Sciences of the United States of America, 90 1
-
J. Langland, L. Langland, C. Zeman, D. Saha, D. Roth (1997)
Developmental regulation of a plant encoded inhibitor of eukaryotic initiation factor 2 alpha phosphorylation.The Plant journal : for cell and molecular biology, 12 2
-
A. Koromilas, Sophie Roy, Sophie Roy, G. Barber, M. Katze, N. Sonenberg (1992)
Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase.Science, 257 5077
-
H. Mellor, C. Proud (1991)
A synthetic peptide substrate for initiation factor-2 kinases.Biochemical and biophysical research communications, 178 2
-
Shuhao Zhu, A. Sobolev, R. Wek (1996)
Histidyl-tRNA Synthetase-related Sequences in GCN2 Protein Kinase Regulate in Vitro Phosphorylation of eIF-2*The Journal of Biological Chemistry, 271
-
G. Kramer, B. Hardesty (1981)
Phosphorylation reactions that influence the activity of elF-2.Current topics in cellular regulation, 20
-
Charles Samuel (1993)
The eIF-2 alpha protein kinases, regulators of translation in eukaryotes from yeasts to humans.The Journal of biological chemistry, 268 11
-
M. Ramírez, R. Wek, C. Aldana, B. Jackson, B. Freeman, A. Hinnebusch (1992)
Mutations activating the yeast eIF-2 alpha kinase GCN2: isolation of alleles altering the domain related to histidyl-tRNA synthetasesMolecular and Cellular Biology, 12
-
S. Lee, M. Esteban (1994)
The interferon-induced double-stranded RNA-activated protein kinase induces apoptosis.Virology, 199 2
-
M. Kawagishi-Kobayashi, J. Silverman, Tekly Ung, T. Dever (1997)
Regulation of the Protein Kinase PKR by the Vaccinia Virus Pseudosubstrate Inhibitor K3L Is Dependent on Residues Conserved between the K3L Protein and the PKR Substrate eIF2 a -
Philip Bevilacqua, Thomas Cech (1996)
Minor-groove recognition of double-stranded RNA by the double-stranded RNA-binding domain from the RNA-activated protein kinase PKR.Biochemistry, 35 31
- Publisher
- Springer Journals
- Copyright
- Copyright © 1999 by Kluwer Academic Publishers
- Subject
- Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
- ISSN
- 0167-4412
- eISSN
- 1573-5028
- DOI
- 10.1023/A:1006379623534
- Publisher site
- See Article on Publisher Site
Abstract
Phosphorylation of the α subunit of eukaryotic initiation factor 2 (eIF2α) is known to be an important translational control mechanism in all eukaryotes with the major exception of plants. Regulation of mammalian and yeast eIF2α activity is directly governed by specific phosphorylation on Ser-51. We now demonstrate that recombinant wheat wild-type (51S) but not mutant 51-Ala (51A) protein is phosphorylated by human PKR and yeast GCN2, which are defined eIF2α kinases. Further, only wheat wild-type eIF2α is a substrate for plant-encoded, double-stranded RNA-dependent kinase (pPKR) activity. Plant PKR and GCN2 phosphorylate recombinant yeast eIF2α 51S but not the 51A mutant demonstrating that pPKR has recognition site capability similar to established eIF2α kinases. A truncated version of wild-type wheat eIF2α containing 51S but not the KGYID motif is not phosphorylated by either hPKR or pPKR suggesting that this putative eIF2α kinase docking domain is essential for phosphorylation. Taken together, these results demonstrate the homology among eukaryotic eIF2α species and eIF2α kinases and support the presence of a plant eIF2α phosphorylation pathway.
Journal
Plant Molecular Biology – Springer Journals
Published: Oct 16, 2004