Endogenous ADP-ribosylation of eukaryotic elongation factor 2 and its 32 kDa tryptic fragment

Ergen K., Bektaş M., Gökçe S., Nurten R.

Biocell, vol.31, no.1, pp.61-66, 2007 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 31 Issue: 1
  • Publication Date: 2007
  • Journal Name: Biocell
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.61-66
  • Keywords: Diphtheria toxin, Endogenous ADP-ribosylation, Eukaryotic elongation factor 2, Protein synthesis, Trypsin digestion
  • İstanbul Yeni Yüzyıl University Affiliated: No

Abstract

Eukaryotic elongation factor 2 (eEF-2) can undergo ADP-ribosylation in the absence of diphtheria toxin. The binding of free ADP-ribose and endogenous transferase-dependent ADP-ribosylation were distinct reactions for eEF-2, as indicated by different findings. Incubation of eEF-2 tryptic fragment 32/33 kDa (32F) with NAD was ADP-ribosylated and gave rise to the covalent binding of ADP-ribose to eEF-2. 32F was revealed to be at the C-terminal by Edman degradation sequence analysis. In our study, the elution of 32F from SDS-PAGE was ADP-ribosylated both in the presence and absence of diphtheria toxin. These results suggest that endogenous ADP-ribosylation of 32F might be related to protein synthesis. This modification appears to be important for the cell function.