Phosphorylation of initiation factor eIF-2 and the control of reticulocyte protein synthesis

@article{Farrell1977PhosphorylationOI,
  title={Phosphorylation of initiation factor eIF-2 and the control of reticulocyte protein synthesis},
  author={Paul J. Farrell and K Balkow and Tim Hunt and Richard J. Jackson and H. Trachsel},
  journal={Cell},
  year={1977},
  volume={11},
  pages={187-200}
}
Regulation of Reticulocyte eIF-2α Kinases by Phosphorylation
TLDR
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 RNA and ATP and its relationship to the interferon-induced mammalian eIF -2α kinase described in other chapters of this book is obvious.
Mode of action of the hemin-controlled inhibitor of protein synthesis.
  • C. de Haro, A. Datta, S. Ochoa
  • Biology, Computer Science
    Proceedings of the National Academy of Sciences of the United States of America
  • 1978
TLDR
A protein is isolated from ribosomal salt washes that enhances the capacity of unphosphorylated eIF-2 to form ternary or 40S initiation complexes but has no effect on the phosphorylated factor.
Regulation of Protein Synthesis in Rabbit Reticulocyte Lysates
TLDR
Observations support the idea that phosphorylation of eIF-2α is not the sole cause (if any) of cessation of protein synthesis in rabbit reticulocyte lysates.
Phosphorylation inhibits guanine nucleotide exchange on eukaryotic initiation factor 2
TLDR
Evidence is presented that the exchange of GTP for GDP bound to eIF-2 is inhibited following phosphorylation of the factor, which may inactivate eif-2 by impairing the ability to recycle between successive rounds of protein synthesis.
Mechanism of translational control by hemin in reticulocyte lysates.
TLDR
In crude preparations from rabbit reticulocyte lysates, hemin inhibits the conversion of proinhibitor to inhibitor catalyzed by endogenous cAMP-dependent protein kinase upon addition of cAMP, but not that caused by the addition of freeprotein kinase catalytic subunit.
Regulation of protein synthesis in rabbit reticulocyte lysates by guanosine triphosphate.
  • R. S. Ranu
  • Biology, Chemistry
    Biochemical and biophysical research communications
  • 1982
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Regulation of protein synthesis in reticulocyte lysates: phosphorylation of methionyl-tRNAf binding factor by protein kinase activity of translational inhibitor isolated from hemedeficient lysates.
TLDR
The observation that the Met-tRNAf binding factor is phosphorylated by PC2 supports the hypothesis that this initiation factor is a target for the action of the translational inhibitor activated in heme deficiency.
Specificity of the protein kinase activity associated with the hemin-controlled repressor of rabbit reticulocyte.
Highly purified preparations of hemin-controlled repressor of rabbit reticulocyte contain a 3':5'-cyclic AMP-indenpendent protein kinase activity that phosphorylates the low-molecular-weight (about
Control of protein synthesis in reticulocyte lysates by haemin.
TLDR
This work examined the formation of complexes between the native subunits present in the lysate and met-tRNAF when lysates were synthesizing protein in the presence and absence of added haemin.
Control of protein synthesis in reticulocyte lysates: effects of 3':5'-cyclic AMP, ATP, and GTP on inhibitions induced by hemedeficiency, double-stranded RNA, and a reticulocyte translationa inhibitor.
TLDR
It is proposed that these inhibitions in reticulocyte lysates involve the phosphorylation by protein kinases of the Met-tRNAf binding factor and/or a related site(s) on the 40S ribosomal subunit and cyclic AMP, GTP, and ATP exert their effects by their actions on this phosphorylated mechanism.
Inhibition of protein synthesis in rabbit reticulocyte lysates by double-stranded RNA and oxidized glutathione: indirect mode of action on polypeptide chain initiation.
TLDR
The inhibitory effects of double-stranded RNA (dsRNA) and oxidized glutathione (GSSG) are partially overcome by a homogeneous initiation factor, IF-MP, which also stimulates protein synthesis in hemin-deficient lysates, and neither dsRNA alone nor GSSG alone significantly inhibits formation of [40S subunit-Met-tRNAf] complexes.
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