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versión impresa ISSN 0327-9545


ERGEN,, Kivanç; BEKTAS¸, Muhammet; GOKCE, Sina  y  NURTEN, Rüstem. Endogenous ADP-ribosylation of eukaryotic elongation factor 2 and its 32 kDa tryptic fragment. Biocell [online]. 2007, vol.31, n.1, pp.61-66. ISSN 0327-9545.

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.

Palabras clave : Eukaryotic elongation factor 2; Endogenous ADP-ribosylation; Protein synthesis; Trypsin digestion; Diphtheria toxin.

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