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Regulation of Reticulocyte eIF-2α Kinases by Phosphorylation

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Translational Regulation of Gene Expression 2

Abstract

Rabbit reticulocytes have served as one of the model systems for studies on eukaryotic protein synthesis for more than three decades. Isolation and characterization of mammalian initiation factors are based to a major extent on results obtained with these cells. In 1975 it was found by Richard Jackson, Tim Hunt, and co-workers that reticulocyte initiation factor 2 (eIF-2) can be phosphorylated in its a subunit. Initial characterization of an apparently unique protein kinase followed.1–4 This enzyme is active in reticulocytes under heme deficiency and leads to cessation of protein synthesis. Without knowing its identity, it had been described several years earlier as the causing agent for inhibition of protein synthesis; it was activated when the postribosomal supernatant was incubated without hemin. The name “heme-controlled repressor” (HCR) had been given to this agent.5 A second protein kinase phosphorylating eIF-2α was found in reticulocytes; it is associated with polysomes and activated by incubation with low concentrations of double-stranded (ds) RNA and ATP.1,6,7 Its relationship to the interferon-induced mammalian eIF-2α kinase described in other chapters of this book is obvious.

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Authors and Affiliations

  1. Department of Chemistry and Biochemistry, and Clayton Foundation Biochemical Institute, University of Texas at Austin, Austin, Texas, 78712, USA

    Gisela Kramer, Wieslaw Kudlicki & Boyd Hardesty

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  1. Gisela Kramer
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  2. Wieslaw Kudlicki
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  1. Institute of Pathology, Case Western Reserve University School of Medicine, Cleveland, Ohio, 44106, USA

    Joseph Ilan

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Kramer, G., Kudlicki, W., Hardesty, B. (1993). Regulation of Reticulocyte eIF-2α Kinases by Phosphorylation. In: Ilan, J. (eds) Translational Regulation of Gene Expression 2. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2894-4_18

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  • DOI: https://doi.org/10.1007/978-1-4615-2894-4_18

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