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


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

BIOCELL, vol.31, no.1, pp.61-66, 2007 (SCI-Expanded) identifier 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
  • Istanbul University Affiliated: Yes

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.