A type 1 phosphoprotein phosphatase active with phosphorylated Mr = 68,000 initiation factor 2 kinase.

@article{Szyszka1989AT1,
  title={A type 1 phosphoprotein phosphatase active with phosphorylated Mr = 68,000 initiation factor 2 kinase.},
  author={R Szyszka and Wieslaw A Kudlicki and Gisela Kramer and B. Hardesty and J Galabru and Ara Hovanessian},
  journal={The Journal of biological chemistry},
  year={1989},
  volume={264 7},
  pages={3827-31}
}
A type 1 protein phosphatase from reticulocytes is shown to efficiently dephosphorylate the Mr = 68,000 phosphopeptide of the double-stranded RNA-dependent kinase that phosphorylates the alpha subunit of eukaryotic peptide initiation factor 2, eIF-2. The kinase, activated in the presence of double-stranded RNA with concomitant phosphorylation of the Mr = 68,000 peptide, causes inhibition of peptide initiation and thereby effects translational control of protein synthesis. The Mn2+-dependent… CONTINUE READING

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