Phosphorylation of only serine-51 in protein synthesis initiation factor-2 is associated with inhibition of peptide-chain initiation in reticulocyte lysates

Nigel T. Price, Gavin I. Welsh, Christopher G. Proud

Research output: Contribution to journalArticle

19 Citations (Scopus)


We have examined the phosphorylation of the α-subunit of initiation factor-2 (eIF-2α) in reticulocyte lysates in which translational shut-off was induced by haem-deficiency or by double-stranded RNA. To maximise the phosphorylation of eIF-2α, lysates were supplemented with the broad spectrum phosphatase inhibitor microcystin. Under all conditions tested, serine-51 was the only residue to become labelled. This is consistent with the observation of only two species of eIF-2α in isoelectric focusing/immunoblotting analyses of lysates treated as described above.

Original languageEnglish
Pages (from-to)993-999
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number3
Publication statusPublished - 15 May 1991
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this