Cytoplasmic inhibitor of eEF-2 ADP-ribosylation catalyzed by diphtheria toxin or endogenous transferase in rat liver cells.
eEF-2 (100 kDa) isolated from rat liver cells undergo ADP-ribosylation in the presence of diphtheria toxin or endogenous ADP-ribosyltransferase, which was co-purified with the factor. We separated the fraction free of elongation factor and endogenous transferase, which strongly inhibited the ADP-ribosylation of eEF-2. This fraction did not affect the activity of the elongation factor. The lack of endogenous transferase activity (which is potentially lethal for the cell) in the postribosomal supernatant could be the result of its inhibition. eEF-2 (65 kDa) which is probably responsible for the process of translocation (Gajko, A. et al. (1999) Biochem. Biophys. Res. Commun. 255, 535-538) was protected from ADP-ribosylation and its irreversible inactivation in the presence of the rat liver extract fraction.
Galicka
A
A
Department of General and Organic Chemistry, Institute of Chemistry, Medical Academy, Bialystok 8, 15-230, Poland.
Sredzińska
K
K
Gindzieński
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A
D000246:Adenosine Diphosphate Ribose / Q000037:antagonists & inhibitors* / Q000378:metabolism; D000818:Animals; D002384:Catalysis; D002478:Cells, Cultured; D004167:Diphtheria Toxin / Q000494:pharmacology*; D008099:Liver / Q000187:drug effects* / Q000201:enzymology / Q000378:metabolism; D008297:Male; D020652:Peptide Elongation Factor 2 / Q000378:metabolism*; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D051381:Rats; D017208:Rats, Wistar
D004167:Diphtheria Toxin; D020652:Peptide Elongation Factor 2; D000246:Adenosine Diphosphate Ribose; D011065:Poly(ADP-ribose) Polymerases