Synthesis and secretion of Bordetella pertussis adenylate cyclase as a 200-kilodalton protein.
Bordetella pertussis, the etiological agent of whooping cough, synthesizes a calmodulin-sensitive adenylate cyclase that is suspected to play a major role in the virulence of this bacterium. We show that adenylate cyclase synthesized as a 200-kilodalton protein is the product of the cyaA gene and that various virulent Bordetella species secrete this high-molecular-weight polypeptide without apparent proteolytic processing. When submitted to trypsin digestion, the 200-kilodalton protein was converted to a stable 45- to 50-kilodalton species. This corresponds to the size of the enzyme previously purified from a culture supernatant. The molecular heterogeneity reported for the various identified forms of adenylate cyclase could therefore result in part from proteolytic degradation or molecular aggregation of the major 200-kilodalton form of the enzyme.
Bellalou
J
J
Unité de Biochimie des Régulations Cellulaires, Institut Pasteur, Paris, France.
Ladant
D
D
Sakamoto
H
H
D000262:Adenylyl Cyclases / Q000096:biosynthesis* / Q000235:genetics / Q000378:metabolism; D000596:Amino Acids / Q000032:analysis; D001426:Bacterial Proteins / Q000378:metabolism / Q000648:ultrastructure; D015153:Blotting, Western; D001886:Bordetella pertussis / Q000201:enzymology* / Q000378:metabolism; D003001:Cloning, Molecular; D005798:Genes, Bacterial; D008970:Molecular Weight; D010449:Peptide Mapping; D015183:Restriction Mapping; D014357:Trypsin / Q000494:pharmacology
D000596:Amino Acids; D001426:Bacterial Proteins; D014357:Trypsin; D000262:Adenylyl Cyclases