Endogenous ADP-ribosylation of eukaryotic elongation factor 2 and its 32 kDa tryptic fragment
| Autor: | Kivanc Ergen, Muhammet Bektaş, Sina Gökçe, Rüstem Nurten |
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| Rok vydání: | 2007 |
| Předmět: |
Diphtheria toxin
ADP Ribose Transferases Adenosine Diphosphate Ribose Glycosylation Edman degradation Sequence analysis Bacterial Toxins Endogeny General Medicine Biology Molecular biology Peptide Fragments Rats Elongation factor Biochemistry Peptide Elongation Factor 2 ADP-ribosylation Protein biosynthesis Animals NAD+ kinase |
| Zdroj: | Biocell : official journal of the Sociedades Latinoamericanas de Microscopia Electronica ... et. al. 31(1) |
| ISSN: | 0327-9545 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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