GTP stabilization of adenylate cyclase activated and ADP-ribosylated by choleragen

Seishi Nakaya, Paul A. Watkins, Alan J. Bitonti, Leonard M Hjelmeland, Joel Moss, Martha Vaughan

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Choleragen activates adenylate cyclase in human skin fibroblasts by catalyzing the ADP-ribosylation of the 42,000 and 47,000 dalton guanyl nucleotide-binding regulatory components (G) of adenylate cyclase. The ADP-ribose linkage to 42,000 and 47,000 dalton proteins was stable at 30°C for 1 h with or without GTP, whereas GTP was required to stabilize activity of the G proteins. In human erythrocytes, choleragen catalyzed the ADP-ribosylation of only a 42,000 dalton G. The ADP-ribosyl-protein linkage was stable for 1 h at 30°C whether or not GTP was present, despite a rapid loss of G activity in the absence of GTP. Inactivation of choleragen-activated G in both the human fibroblast and human erythrocyte is, therefore, not secondary to the de-ADP-ribosylation of specifically labeled G subunits.

Original languageEnglish (US)
Pages (from-to)66-74
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume102
Issue number1
DOIs
StatePublished - Sep 16 1981
Externally publishedYes

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Cholera Toxin
Guanosine Triphosphate
Adenylyl Cyclases
Adenosine Diphosphate
Stabilization
Fibroblasts
Erythrocytes
Adenosine Diphosphate Ribose
GTP-Binding Proteins
Skin
Proteins
Nucleotides

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

GTP stabilization of adenylate cyclase activated and ADP-ribosylated by choleragen. / Nakaya, Seishi; Watkins, Paul A.; Bitonti, Alan J.; Hjelmeland, Leonard M; Moss, Joel; Vaughan, Martha.

In: Biochemical and Biophysical Research Communications, Vol. 102, No. 1, 16.09.1981, p. 66-74.

Research output: Contribution to journalArticle

Nakaya, Seishi ; Watkins, Paul A. ; Bitonti, Alan J. ; Hjelmeland, Leonard M ; Moss, Joel ; Vaughan, Martha. / GTP stabilization of adenylate cyclase activated and ADP-ribosylated by choleragen. In: Biochemical and Biophysical Research Communications. 1981 ; Vol. 102, No. 1. pp. 66-74.
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