Journal article
Cholera toxin and pertussis toxin substrates and endogenous ADP-ribosyltransferase activity in Drosophila melanogaster
Biochimica et biophysica acta. Molecular cell research, Vol.970(3), pp.355-362
1988
DOI: 10.1016/0167-4889(88)90135-8
PMID: 3135838
Abstract
Cholera toxin- and pertussis toxin-catalyzed ADP-ribosylation were used to identify and localize G protein substrates in
Drosophila melanogaster and in
Manduca sexta. Cholera toxin catalyzes ADP-ribosylation of 37 kDa and 50 kDa polypeptides, but these polypeptides are also substrates for an ADP-ribosyltransferase (EC 2.4.2.30) activity endogenous to the
Drosophila extracts. Pertussis toxin modifies 37 kDa and 39 kDa polypeptides in
Drosophila homogenates. The pattern of proteolysis of the 39 kDa pertussis toxin substrate is similar to that of mammalian G
o and is influenced by guanyl nucleotide binding. The 39 kDa G
o-like
Drosophila and
Manduca pertussis toxin substrates are found primarily in neural tissues. These studies provide further evidence that G proteins are present in
Drosophila and that this organism can therefore be used to investigate the physiological roles of these enzymes using advanced genetic manipulations.
Details
- Title: Subtitle
- Cholera toxin and pertussis toxin substrates and endogenous ADP-ribosyltransferase activity in Drosophila melanogaster
- Creators
- Rosemary S. Hopkins - California Institute of TechnologyMark A. Stamnes - University of WashingtonMelvin I. Simon - California Institute of TechnologyJames B. Hurley - Howard Hughes Medical Institute
- Resource Type
- Journal article
- Publication Details
- Biochimica et biophysica acta. Molecular cell research, Vol.970(3), pp.355-362
- Publisher
- Elsevier B.V
- DOI
- 10.1016/0167-4889(88)90135-8
- PMID
- 3135838
- ISSN
- 0167-4889
- eISSN
- 1879-2596
- Language
- English
- Date published
- 1988
- Academic Unit
- Molecular Physiology and Biophysics; Internal Medicine
- Record Identifier
- 9984297609902771
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