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    
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).
J Avigan; J J Murtagh; L A Stevens; C W Angus; J Moss; M Vaughan
Related Documents :
1052599 - Possible mechanism of photophosphorylation in rhodopseudomonas viridis.
22701449 - Microbial group specific uptake kinetics of inorganic phosphate and adenosine-5'-tripho...
15478799 - Adenylate kinase and gtp:amp phosphotransferase of the malarial parasite plasmodium fal...
2167269 - Hypochlorite-modified adenine nucleotides: structure, spin-trapping, and formation by a...
20092359 - Crystal structure of the catalytic domain of human parp2 in complex with parp inhibitor...
166989 - Electron paramagnetic resonance and water proton relaxation rate studies of formyltetra...
11742119 - N-terminal contributions of the gamma-subunit of fetal hemoglobin to its tetramer stren...
23667909 - Mast cells limit extracellular levels of il-13 via a serglycin proteoglycan-serine prot...
18796559 - Minimal length requirement for proteasomal degradation of ubiquitin-dependent substrates.
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    
Laboratory of Cellular Metabolism, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Adenosine Diphosphate Ribose / metabolism*
Base Sequence
Cloning, Molecular
Escherichia coli / genetics
GTP-Binding Proteins / genetics,  isolation & purification,  metabolism*
Genetic Vectors
Macromolecular Substances
Molecular Sequence Data
Mutagenesis, Site-Directed*
NAD / metabolism*
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*
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 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

Previous Document:  Unusual secondary specificity of prolyl oligopeptidase and the different reactivities of its two for...
Next Document:  Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments.