| First Author | Moehring JM | Year | 1988 |
| Journal | J Biol Chem | Volume | 263 |
| Issue | 8 | Pages | 3840-4 |
| PubMed ID | 3346227 | Mgi Jnum | J:354361 |
| Mgi Id | MGI:7734755 | Citation | Moehring JM, et al. (1988) The post-translational trimethylation of diphthamide studied in vitro. J Biol Chem 263(8):3840-4 |
| abstractText | The amino acid diphthamide is a complex post-translational derivative of histidine that exists in eukaryotic and Archaebacterial elongation factor 2 (EF-2). Diphtheria toxin and Pseudomonas exotoxin A catalyze the transfer of an ADP-ribose residue from NAD to diphthamide, causing the inactivation of EF-2. We have used cytosolic extracts of mutant CHO-K1 cells to study the biosynthesis of diphthamide in vitro. We have identified chromatographically a precursor form of diphthamide that exists in one complementation group of mutant cells and have documented the addition of 3 methyl residues from S-adenosylmethionine to this precursor. We have identified the presence of methyltransferase capable of carrying out this reaction in vitro in cells of 15 diverse eukaryotic species. |
