The protein cofactor necessary for ADP-ribosylation of G(s) by cholera toxin is itself a GTP binding protein

R. A. Kahn, A. G. Gilman

Research output: Contribution to journalArticle

346 Citations (Scopus)

Abstract

A membrane-bound protein cofactor (ARF) is required for the cholera toxin-dependent ADP-ribosylation of the stimulatory regulatory component (G(s)) of adenylate cyclase. Improved methods for the purification of ARF from bovine brain are described. ARF has a high-affinity binding site for guanine nucleotides. Binding of GTP or GTPγS to ARF is necessary for the activity of the cofactor; GDP·ARF does not support ADP-ribosylation of G(s). Although the protein as purified contains stoichiometric amounts of GDP, GTPase activity of isolated ARF was not detected. Cholera toxin-dependent activation of adenylate cyclase thus requires two guanine nucleotide binding proteins.

Original languageEnglish (US)
Pages (from-to)7906-7911
Number of pages6
JournalJournal of Biological Chemistry
Volume261
Issue number17
StatePublished - 1986

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Guanine Nucleotides
Cholera Toxin
GTP-Binding Proteins
Adenylyl Cyclases
Adenosine Diphosphate
CD46 Antigens
ADP-Ribosylation Factors
GTP Phosphohydrolases
Guanosine Triphosphate
Purification
Brain
Carrier Proteins
Proteins
Chemical activation
Binding Sites
Membranes

ASJC Scopus subject areas

  • Biochemistry

Cite this

The protein cofactor necessary for ADP-ribosylation of G(s) by cholera toxin is itself a GTP binding protein. / Kahn, R. A.; Gilman, A. G.

In: Journal of Biological Chemistry, Vol. 261, No. 17, 1986, p. 7906-7911.

Research output: Contribution to journalArticle

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