Translational control of ADP-ribosylation in eucaryotic cells.
Starvation of the mouse hepatoma cell line Hepa for an essential amino acid (Trp, His, Leu, Ile or Phe) stimulated the incorporation of [3H]adenosine as ADP-ribose monomer into an 80,000-Mr protein, P80. Two-dimensional electrophoresis of Hepa proteins showed that P80 was the only protein labeled under starvation conditions. Time course experiments showed that the ADP-ribosylation of P80 was a consequence rather than the cause of reduced translational activity. Cycloheximide treatment and incubation at reduced temperatures also reduced the rate of protein synthesis and stimulated the ADP-ribosylation of P80. Starvation-dependent ADP-ribosylation of P80 was shown to occur in three other cell lines (Chang, Neuro-2a, and chick comb fibroblasts).
D000241:Adenosine / Q000378:metabolism; D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000601:Amino Acids, Essential / Q000502:physiology; D002460:Cell Line; D003080:Cold Temperature; D003513:Cycloheximide / Q000494:pharmacology; D011132:Polyribosomes / Q000378:metabolism; D014176:Protein Biosynthesis; D011506:Proteins / Q000378:metabolism; D014364:Tryptophan / Q000502:physiology
D000601:Amino Acids, Essential; D011506:Proteins; D000246:Adenosine Diphosphate Ribose; D014364:Tryptophan; D003513:Cycloheximide; D000241:Adenosine