Binding of ATP by pertussis toxin and isolated toxin subunits

The binding of ATP to pertussis toxin and its components, the A subunit and B oligomer, was investigated. Whereas, radiolabeled ATP bound to the B oligomer and pertussis toxin, no binding to the A subunit was observed. The binding of [3H]ATP to pertussis toxin and the B oligomer was inhibited by nuc...

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Bibliographic Details
Published in:Biochemistry (Easton) 1990-07, Vol.29 (26), p.6128-6131
Main Authors: Hausman, Sally Z, Manclark, Charles R, Burns, Drusilla L
Format: Article
Language:English
Subjects:
550201 - Biochemistry- Tracer Techniques
Adenosine Triphosphate - metabolism
alpha-Fetoproteins - metabolism
ANTIGENS
ATP
BACTERIA
Bacteriology
BASIC BIOLOGICAL SCIENCES
Binding Sites
Binding, Competitive
BIOCHEMICAL REACTION KINETICS
Biological and medical sciences
CHARGED PARTICLES
CHEMICAL REACTIONS
CROSS-LINKING
Fundamental and applied biological sciences. Psychology
HYDROGEN COMPOUNDS
IONS
KINETICS
MATERIALS
Microbiology
MICROORGANISMS
NAD - metabolism
NUCLEOTIDES
Nucleotides - metabolism
ORGANIC COMPOUNDS
OXYGEN COMPOUNDS
Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains
Peptide Fragments - metabolism
Pertussis Toxin
PHOSPHATES
Phosphates - metabolism
PHOSPHORUS COMPOUNDS
POLYMERIZATION
Protein Binding
REACTION KINETICS
TOXIC MATERIALS
TOXINS
TRITIUM COMPOUNDS
Virulence Factors, Bordetella - metabolism
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Description
Summary:The binding of ATP to pertussis toxin and its components, the A subunit and B oligomer, was investigated. Whereas, radiolabeled ATP bound to the B oligomer and pertussis toxin, no binding to the A subunit was observed. The binding of [3H]ATP to pertussis toxin and the B oligomer was inhibited by nucleotides. The relative effectiveness of the nucleotides was shown to be ATP greater than ATP greater than GTP greater than CTP greater than TTP for pertussis toxin and ATP greater than GTP greater than TTP greater than CTP for the B oligomer. Phosphate ions inhibited the binding of [3H]ATP to pertussis toxin in a competitive manner; however, the presence of phosphate ions was essential for binding of ATP to the B oligomer. The toxin substrate, NAD, did not affect the binding of [3H]ATP to pertussis toxin, although the glycoprotein fetuin significantly decreased binding. These results suggest that the binding site for ATP is located on the B oligomer and is distinct from the enzymatically active site but may be located near the eukaryotic receptor binding site.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00478a003