Phosphorylation of elongation factor 1 in polyribosome fraction of rabbit reticulocytes

FEBS Lett. 1984 Oct 29;176(2):401-5. doi: 10.1016/0014-5793(84)81206-5.

Abstract

A single protein, Mr approximately 50000, is shown to be phosphorylated during incubation of a mono- and polyribosome fraction of rabbit reticulocytes with [gamma-32P]ATP at a low ionic strength. This protein has been identified as the elongation factor 1 alpha (EF-1 alpha). The phosphorylated EF-1 alpha, in contrast to the unmodified factor, is not detected in complexes with mono- and polyribosomes. It is suggested that the phosphorylation of EF-1 alpha can result in its decompartmentation from polyribosomes and thus affect the rate of protein synthesis.

MeSH terms

  • Animals
  • Centrifugation, Density Gradient
  • Molecular Weight
  • Osmolar Concentration
  • Peptide Elongation Factor 1
  • Peptide Elongation Factors / metabolism*
  • Phosphorylation
  • Polyribosomes / metabolism*
  • Rabbits
  • Reticulocytes / metabolism*
  • Reticulocytes / ultrastructure

Substances

  • Peptide Elongation Factor 1
  • Peptide Elongation Factors