Identification of the phosphorylation sites in elongation factor-2 from rabbit reticulocytes

Nigel T. Price, Nicholas T. Redpath, Konstantin V. Severinov, David G. Campbell, J. M. Russell, Christopher G. Proud

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Abstract

The sites in eukaryotic elongation factor eEF-2 phosphorylated by the Ca2+/calmodulin-dependent eEF-2 kinase in vitro have been identified. The kinase catalysed the rapid incorporation of one mol of phosphate per mol eEF-2 and the slower incorporation of a second mol. All the phosphorylation sites in eEF-2 are contained in the CNBr fragment corresponding to residues 22-155. Tryptic digestion of phosphorylated eEF-2 yielded 3 phosphopeptides, one being unique to monophosphorylated eEF-2. The phosphorylation sites were identified as threonine residues 56 and 58, the former being more rapidly phosphorylated. Ala-Gly-Glu-Thr-Phe-Thr14-Asp-Thr18-Arg. The same sites are labelled in eEF-2 isolated from reticulocyte lysates.

Original languageEnglish
Pages (from-to)253-258
Number of pages6
JournalFEBS Letters
Volume282
Issue number2
DOIs
Publication statusPublished - 6 May 1991

Keywords

  • Calcium/calmodulin
  • Elongation factor-2
  • Protein kinase
  • Protein phosphorylation
  • Protein synthesis
  • Rabbit reticulocyte

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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