Cellular mono(ADP-ribosyl) transferase inhibits protein synthesis.
A reticulocyte translation system was depleted of functional EF-2 by treatment with diphtheria toxin (DT) fragment A and NAD. After dialysis to remove NAD, the system was reconstituted using preparations of EF-2 derived from pyBHK cells. Untreated and reconstituted lysates permitted similar rates of translation. As expected, when DT-treated EF-2 was used to reconstitute the system, no translation occurred. Furthermore EF-2, reacting with the endogenous ADP-ribosyl transferase from pyBHK cells, was also unable to restore protein synthesis in the reconstituted system. These studies suggest that eukaryotic cellular ADP-ribosyl transferases may play a role in regulating protein synthesis.
Iglewski
W J
WJ
Department of Microbiology and Immunology, University of Rochester Medical Center, NY 14642.
Dewhurst
S
S
D036002:ADP Ribose Transferases; D000595:Amino Acid Sequence; D000818:Animals; D001427:Bacterial Toxins; D002460:Cell Line; D002474:Cell-Free System; D004167:Diphtheria Toxin / Q000235:genetics / Q000494:pharmacology; D005098:Exotoxins / Q000235:genetics; D007700:Kinetics; D008969:Molecular Sequence Data; D009243:NAD / Q000378:metabolism / Q000494:pharmacology; D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors / Q000235:genetics / Q000378:metabolism; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D014176:Protein Biosynthesis; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism; D012689:Sequence Homology, Nucleic Acid; D037521:Virulence Factors; D000097668:Pseudomonas aeruginosa Exotoxin A
D036002:ADP Ribose Transferases; D001427:Bacterial Toxins; D004167:Diphtheria Toxin; D005098:Exotoxins; D009243:NAD; D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors; D011065:Poly(ADP-ribose) Polymerases; D037521:Virulence Factors; D000097668:Pseudomonas aeruginosa Exotoxin A