Endogenous ADP-ribosylation of eukaryotic elongation factor 2 and its 32 kDa tryptic fragment.
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.
Ergen
Kivanç
K
Kocaeli University Medical Faculty, Department of Biophysics, 41380 Umuttepe, Izmit-Kocaeli, Turkey. kergen@hotmail.com
Bektaş
Muhammet
M
Gökçe
Sina
S
Nurten
Rüstem
R
D036002:ADP Ribose Transferases; D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000818:Animals; D001427:Bacterial Toxins / Q000378:metabolism; D006031:Glycosylation; D020652:Peptide Elongation Factor 2 / Q000302:isolation & purification* / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism; D051381:Rats
D001427:Bacterial Toxins; D020652:Peptide Elongation Factor 2; D010446:Peptide Fragments; D000246:Adenosine Diphosphate Ribose; D036002:ADP Ribose Transferases