Open Access

ARTICLE

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

KIVANÇ ERGEN^*, MUHAMMET BEKTAŞ^**, SINA GÖKÇE^**, RÜSTEM NURTEN^**

* Kocaeli University Medical Faculty, Department of Biophysics, 41380 Umuttepe, Izmit-Kocaeli, TURKEY.
** Istanbul University Istanbul Faculty of Medicine, Department of Biophysics, 34390 Çapa-Ístanbul, TURKEY
Address correspondence to: Dr. Kivanç Ergen. Kocaeli University Medical Faculty, Department of Biophysics, 41380 Umuttepe, Ízmit-Kocaeli, TURKEY. Phone: (+90 262) 303 84 97. E-mail: kergen@hotmail.com

BIOCELL 2007, 31(1), 61-66. https://doi.org/10.32604/biocell.2007.31.061

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.

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