Phosphorylation of elongation factor 1 beta by an endogenous kinase affects its catalytic nucleotide exchange activity

J Biol Chem. 1988 Aug 15;263(23):11063-6.


Elongation factor 1 beta (EF-1 beta) from Artemia is phosphorylated to a high percentage at serine 89 by an endogenous kinase present in EF-1 beta gamma. Protein sequencing of EF-1 beta revealed that this serine residue is located N-terminally of an acidic cluster of amino acids, (formula; see text) which is critical for casein kinase II-type substrate recognition. A number of compounds known to influence casein kinases were studied, revealing that the kinase activity as present in EF-1 beta gamma belongs to the class of casein kinase II. The rate of nucleotide exchange on EF-1 alpha as catalyzed by EF-1 beta was found to be affected reversibly by the state of phosphorylation of EF-1 beta. In the presence of dephosphorylated EF-1 beta, the exchange rate is almost twice as large compared to the rate in the presence of phosphorylated EF-1 beta. Rephosphorylation of dephosphorylated EF-1 beta diminishes the activity of the protein again. The role of casein kinase II-type enzymes in modulating the function of proteins involved in polypeptide synthesis is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Artemia
  • Isoelectric Focusing
  • Peptide Elongation Factor 1
  • Peptide Elongation Factors / metabolism*
  • Peptide Fragments / analysis
  • Phosphorylation
  • Protein Kinases / metabolism*
  • Trypsin / metabolism


  • Peptide Elongation Factor 1
  • Peptide Elongation Factors
  • Peptide Fragments
  • Protein Kinases
  • Trypsin