The 65-kDa protein from pig heart A new substrate for Clostridium botulinum ADP-ribosyltransferase (exoenzyme C 3)

• Published in: FEBS letters Vol. 293; no. 1; pp. 59 - 61
• Main Authors: Hoffenberg, Simon I., Rybin, Vitalyi O., Efimenko, Alexander N., Kurochkin, Iliya N., Tkachuk, Vsevolod A.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 18.11.1991; Elsevier
• Subjects: ADP Ribose Transferases - isolation & purification; ADP Ribose Transferases - metabolism; ADP-ribosylation; ADP-ribosyltransferase; Analytical, structural and metabolic biochemistry; Animals; Bacterial Proteins - chemistry; Bacterial Proteins - isolation & purification; Biological and medical sciences; Botulinum Toxins; Clostridium botulinum; Clostridium botulinum - chemistry; Clostridium botulinum - enzymology; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; GTP-binding protein; GTP-Binding Proteins - analysis; heart; Heart Ventricles - chemistry; Hydrolysis; identification; mediation; Molecular Weight; NAD super(+) ADP-ribosyltransferase; Pig heart sarcolemma; pigs; proteins; sarcolemma; Sarcolemma - chemistry; Substrate Specificity; Swine; Transferases; ADP-ribosyltransferase; GTP-binding protein; Clostridium botulinum; Pig heart sarcolemma; Heart; Sarcolemma; GTP; Enzyme; Clostridiales; Pig; Characterization; Substrate; Binding protein; Vertebrata; Mammalia; Proteolysis; Clostridiaceae; Bacteria; Artiodactyla; Ungulata
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(91)81152-X

In the pig heart sarcolemma, a 65 kDa protein is found to be ADP-ribosylated by Clostridium botulinum ADP-ribosyltransferase (exoenzyme C 3). ADP-ribosylation of this protein is regulated by guanyl nucleotides and cytosol factor in a fashion similar to that for other C 3 substrates. The new exoenzyme C 3 substrate was partially purified. This protein is supposed to be a GTP-binding one.