Endogenous ADP-ribosylation for eukaryotic elongation factor 2: evidence of two different sites and reactions
| Autor: | Kivanc Ergen, Engin Bermek, Muhammet Bektaş, Rüstem Nurten |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Clinical Biochemistry
Endogeny Biology Biochemistry chemistry.chemical_compound Peptide Elongation Factor 2 Protein biosynthesis Animals Transferase Diphtheria Toxin Carbon Radioisotopes ADP Ribose Transferases Diphtheria toxin Adenosine Diphosphate Ribose Diphthamide Cell Biology General Medicine Rats Elongation factor Liver chemistry ADP-ribosylation Chromatography Thin Layer NAD+ kinase Protein Processing Post-Translational |
| Zdroj: | Cell Biochemistry and Function. 24:369-380 |
| ISSN: | 1099-0844 0263-6484 |
| DOI: | 10.1002/cbf.1265 |
| Popis: | Eukaryotic elongation factor 2 can undergo ADP-ribosylation in the absence of diphtheria toxin under the action of an endogenous transferase. The investigation which aimed to gain insight into the nature of endogenous ADP-ribosylation revealed that this reaction may be, in some cases, due to covalent binding of free ADP-ribose to elongation factor 2. Binding of free ADP-ribose, and NAD- and endogenous transferase-dependent ADP-ribosylation were suggested to be distinct reactions by different findings. Free ADP-ribose could bind to elongation factor 2 previously subjected to ADP-ribosylation by diphtheria toxin or endogenous transferase. The binding of free ADP-ribose was inhibited by neutral NH2OH, L-lysine and picrylsulfonate, whereas endogenous ADP-ribosyltransferase was inhibited by NAD glycohydrolase inhibitors and L-arginine. The ADP-ribosyl-elongation factor 2 adduct which formed upon binding of free ADP-ribose was resistant to neutral NH2OH, but decomposed almost completely upon treatment with NaOH. The product of endogenous transferase-dependent ADP- ribosylation was partially resistant to NH2OH and NaOH treatment. Moreover, this reaction was reversed in the presence of diphtheria toxin and nicotinamide. Both types of endogenous ADP-ribosylation gave rise to inhibition of polyphenylalanine synthesis. This study thus provides evidence for the presence of two different types of endogenous ADP-ribosylation of eukaryotic elongation factor 2. The respective sites involved in these reactions are distinct from one another as well as from diphthamide, the site of attack by diphtheria toxin. |
| Databáze: | OpenAIRE |
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