Document Detail


Pertussis toxin-catalyzed ADP-ribosylation of G(o) alpha with mutations at the carboxyl terminus.
MedLine Citation:
PMID:  1510959     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The guanine nucleotide-binding protein G(o alpha) has been implicated in the regulation of Ca2+ channels in neural tissues. Covalent modification of G(o alpha) by pertussis toxin-catalyzed ADP-ribosylation of a cysteine (position 351) four amino acids from the carboxyl terminus decouples G(o alpha) from receptor. To define the structural requirements for ADP-ribosylation, preparations of recombinant G(o alpha) with mutations within the five amino acids at the carboxyl terminus were evaluated for their ability to serve as pertussis toxin substrates. As expected, the mutant in which cysteine 351 was replaced by glycine (C351G) was not a toxin substrate. Other inactive mutants were G352D and L353 delta/Y354 delta. Mutations that had no significant effect on toxin-catalyzed ADP-ribosylation included G350D, G350R, Y354 delta, and L353V/Y354 delta. Less active mutants were L353G/Y354 delta, L353A/Y354 delta, and L353G. ADP-ribosylation of the active mutants, like that of wild-type G(o alpha), was enhanced by the beta gamma subunits of bovine transducin. It appears that three of the four terminal amino acids critically influence pertussis toxin-catalyzed ADP-ribosylation of G(o alpha).
Authors:
J Avigan; J J Murtagh; L A Stevens; C W Angus; J Moss; M Vaughan
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochemistry     Volume:  31     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1992 Aug 
Date Detail:
Created Date:  1992-09-29     Completed Date:  1992-09-29     Revised Date:  2006-04-21    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  7736-40     Citation Subset:  IM    
Affiliation:
Laboratory of Cellular Metabolism, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Diphosphate Ribose / metabolism*
Animals
Base Sequence
Cattle
Cloning, Molecular
Escherichia coli / genetics
GTP-Binding Proteins / genetics,  isolation & purification,  metabolism*
Genetic Vectors
Macromolecular Substances
Molecular Sequence Data
Mutagenesis, Site-Directed*
NAD / metabolism*
Oligodeoxyribonucleotides
Pertussis Toxin*
Polymerase Chain Reaction / methods
Recombinant Proteins / isolation & purification,  metabolism
Restriction Mapping
Retina / metabolism
Substrate Specificity
Transducin / isolation & purification,  metabolism
Virulence Factors, Bordetella / metabolism,  pharmacology*
Chemical
Reg. No./Substance:
0/Macromolecular Substances; 0/Oligodeoxyribonucleotides; 0/Recombinant Proteins; 0/Virulence Factors, Bordetella; 20762-30-5/Adenosine Diphosphate Ribose; 53-84-9/NAD; EC 2.4.2.31/Pertussis Toxin; EC 3.6.1.-/GTP-Binding Proteins; EC 3.6.1.-/Transducin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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