eEF2 diphthamide modification restrains spurious frameshifting to maintain translational fidelity

• Published in: Nucleic acids research Vol. 51; no. 13; pp. 6899 - 6913
• Main Authors: Shin, Byung-Sik, Ivanov, Ivaylo P, Kim, Joo-Ran, Cao, Chune, Kinzy, Terri G, Dever, Thomas E
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 21.07.2023
• Subjects: Animals; Bacterial Toxins - metabolism; Codon, Terminator - metabolism; Frameshifting, Ribosomal; Mammals - genetics; Nucleic Acid Enzymes; Peptide Elongation Factor 2 - chemistry; Protein Biosynthesis; Saccharomyces cerevisiae - metabolism

Abstract Diphthamide (DPH), a conserved amino acid modification on eukaryotic translation elongation factor eEF2, is synthesized via a complex, multi-enzyme pathway. While DPH is non-essential for cell viability and its function has not been resolved, diphtheria and other bacterial toxins ADP-ribosy...