Casein kinase-2 phosphorylates serine-2 in the β-subunit of initiation factor-2

Stephanie J. Clark, Anthony J. Ashford, Nigel T. Price, Christopher G. Proud

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We have previously presented evidence which suggests that casein kinase-2 phosphorylates a serine residue near the N-terminus of the β-subunit of the initiation factor eIF-2 (Clark, S.J. et al. Biochim. Biophys. Acta 968, 211-219). We now report further data which confirm that it is serine-2 which is phosphorylated by casein kinase-2. This data includes (1) the electrophoretic mobilities of the phosphopeptides produced by different cleavage techniques, (2) the amino acid composition of the principal phosphopeptide generated by treatment with cyanogen bromide and (3) the resistance of this phosphopeptide to Edman degradation.

Original languageEnglish
Pages (from-to)377-380
Number of pages4
JournalBBA - Molecular Cell Research
Issue number3
Publication statusPublished or Issued - 6 Mar 1989
Externally publishedYes


  • Casein kinase-2
  • Initiation factor
  • Protein phosphorylation
  • Protein synthesis

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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