Purification and activation of the double-stranded RNA-dependent eIF-2 kinase DAI. [PDF]
Molecular and Cellular Biology, 1989 The double-stranded RNA (dsRNA)-dependent protein kinase DAI (also termed dsI and P1) possesses two kinase activities; one is an autophosphorylation activity, and the other phosphorylates initiation factor eIF-2. We purified the enzyme, in a latent form, to near homogeneity from interferon-treated human 293 cells.
Matthew J. Kostura, Michael B. Mathews
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Disulfide Bond Formation in the Regulation of eIF-2 α Kinase by Heme
Journal of Biological Chemistry, 1989 Abstract The inhibition of the autophosphorylation of the heme-regulated eukaryotic initiation factor (eIF)-2 alpha kinase (HRI) by hemin is very similar to that produced by thiol oxidation by diamide. The results obtained from the analysis of sodium dodecyl sulfate-polyacrylamide gel electrophoresis of unphosphorylated and phosphorylated HRI under ...
J J Chen +4 more
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Cloning of the cDNA of the heme-regulated eukaryotic initiation factor 2 alpha (eIF-2 alpha) kinase of rabbit reticulocytes: homology to yeast GCN2 protein kinase and human double-stranded-RNA-dependent eIF-2 alpha kinase. [PDF]
Proceedings of the National Academy of Sciences, 1991 We have cloned the cDNA of the heme-regulated eIF-2 alpha kinase (HRI) of rabbit reticulocytes. In vitro translation of mRNA transcribed from the HRI cDNA yields a 90-kDa polypeptide that exhibits eIF-2 alpha kinase activity and is recognized by a monoclonal antibody directed against authentic HRI.
J J Chen +6 more
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Regulation of eukaryotic protein synthesis by protein kinases that phosphorylate initiation factor eIF-2 [PDF]
Molecular Biology Reports, 1994 Michael J. Clemens
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Erythroid expression of the heme-regulated eIF-2 alpha kinase. [PDF]
Molecular and Cellular Biology, 1994 The role of heme-regulated eIF-2 alpha kinase (HRI) in the regulation of protein synthesis in rabbit reticulocytes is well documented. Inhibitors of protein synthesis with properties similar to those of HRI have been described in some nonerythroid cell types, but it has not yet been determined whether these eIF-2 alpha kinase activities are mediated by
John S. Crosby +3 more
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Histidyl-tRNA Synthetase-related Sequences in GCN2 Protein Kinase Regulate in Vitro Phosphorylation of eIF-2 [PDF]
Journal of Biological Chemistry, 1996 In yeast, starvation for amino acids stimulates GCN2 phosphorylation of the alpha subunit of eukaryotic initiation factor-2 (eIF-2). Phosphorylation of eIF-2alpha induces the translational expression of GCN4, a transcriptional activator of the general amino acid control pathway.
Shuhao Zhu +2 more
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Journal of Biological Chemistry, 1989 We have reported previously that a 67-kDa polypeptide (p67) present in reticulocyte lysates protects the alpha-subunit of reticulocyte eukaryotic peptide chain initiation factor 2 (eIF-2) from phosphorylation by an eIF-2 kinase, heme-regulated protein synthesis inhibitor (Datta, B., Chakrabarti, D., Roy, A.L., and Gupta, N. K. (1988) Proc. Natl.
B Datta +4 more
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Sensory Denervation Modulates eIF-2 Alpha Kinase Expression in the Rabbit Lacrimal Gland [PDF]
Current Eye Research, 2006 To investigate the hypothesis that sensory denervation of the rabbit lacrimal gland results in dysregulation of protein synthesis. We used differential display of mRNA to identify genes associated with protein synthesis and secretion that may be altered in this situation.New Zealand white rabbits underwent unilateral sensory denervation by the ablation
Doan Nguyen +3 more
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Generation of a Mutant Form of Protein Synthesis Initiation Factor eIF-2 Lacking the Site of Phosphorylation by eIF-2 Kinases [PDF]
Molecular and Cellular Biology, 1988 The phosphorylation of the alpha-subunit of initiation factor eIF-2 leads to an inhibition of protein synthesis in mammalian cells. We have performed site-directed mutagenesis on a cDNA encoding the alpha-subunit of human eIF-2 and have replaced the candidate sites of phosphorylation, Ser-48 and Ser-51, with alanines.
Vinay K. Pathak +2 more
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