Effect of ADP-ribosylation factor amino-terminal deletions on its GTP-dependent stimulation of cholera toxin activity.
J Biol Chem
; 269(13): 9743-5, 1994 Apr 01.
Article
em En
| MEDLINE
| ID: mdl-8144566
ABSTRACT
It has been proposed that the amino-terminal domain of ADP-ribosylation factor (ARF) is critical for its stimulation of cholera toxin ADP-ribosyltransferase activity. In this study, recombinant ARF1 (rARF1), r delta 13ARF1 (recombinant ARF1 lacking the first 13 amino acids) and rPKA14ARF1 (recombinant ARF1 in which the first 14 amino acids were replaced by the first 7 amino acids of the cAMP-dependent protein kinase catalytic subunit) were used to assess the effect of the amino terminus on the ability of ARF to enhance ADP-ribosylation of agmatine by the cholera toxin A subunit. The GTP-dependent ARF activities of r delta 13ARF1 and rPKA14ARF1 were similar to that of rARF1, whereas the GTP requirement for half-maximal activation of cholera toxin A, was somewhat higher for rARF1 than it was for r delta 13ARF1 and rPKA14ARF1. These results are consistent with the view that the amino terminus of ARF1 is not critical for its action as a GTP-dependent activator of cholera toxin.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Toxina da Cólera
/
Proteínas de Ligação ao GTP
/
Guanosina Trifosfato
Limite:
Humans
Idioma:
En
Revista:
J Biol Chem
Ano de publicação:
1994
Tipo de documento:
Article