Endogenous ADP-ribosylation of eukaryotic elongation factor 2 and its 32 kDa tryptic fragment
Biocell
; 31(1): 61-66, abr. 2007. ilus
Article
in En
| LILACS
| ID: lil-491538
Responsible library:
AR40.1
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.
Full text:
1
Collection:
01-internacional
Database:
LILACS
Main subject:
Bacterial Toxins
/
Glycosylation
/
Adenosine Diphosphate Ribose
/
ADP Ribose Transferases
Limits:
Animals
Language:
En
Journal:
Biocell
Journal subject:
Clulas
Year:
2007
Document type:
Article
Affiliation country:
Turquía
Country of publication:
Argentina