Phosphorylation of elongation factor 1 in polyribosome fraction of rabbit reticulocytes.
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.
D000818:Animals; D002499:Centrifugation, Density Gradient; D008970:Molecular Weight; D009994:Osmolar Concentration; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors / Q000378:metabolism*; D010766:Phosphorylation; D011132:Polyribosomes / Q000378:metabolism*; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism* / Q000648:ultrastructure
D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors